Ribonuclease activity in cell-free thymus homogenates was elevated for five strains of mice genetically predisposed toward leukemia or reticulum cell neoplasms (AKR, C58, PL, RF, and SJL). Such increased activity was directed against polyuridylic acid and was observed in 8-wk old mice, well before the onset of neoplastic transformation. Similarly, white blood cell ribonuclease activity was elevated in mice of the strains AKR, C2H/He, PL and RF. Statistical analysis indicated that such elevated activity in these strains related to their high incidence of spontaneous neoplastic disease. Elevated ribonuclease activity thus represents a new biochemical marker relating to the genetic propensity of some strains of mice to die prematurely of spontaneous neoplasia. ...
The affinity of RI for ribonucleases is among the highest for any protein-protein interaction; the dissociation constant of the RI-RNase A complex is in the femtomolar (fM) range under physiological conditions while that for the RI-angiogenin complex is less than 1 fM. Despite this high affinity, RI is able to bind a wide variety of RNases A despite their relatively low sequence identity. Both biochemical studies and crystallographic structures of RI-RNase A complexes suggest that the interaction is governed largely by electrostatic interactions, but also involves substantial buried surface area.[3][4] RIs affinity for ribonucleases is important, since many ribonucleases have cytotoxic and cytostatic effects that correlate well with ability to bind RI.[5] Mammalian RIs are unable to bind certain pancreatic ribonuclease family members from other species. In particular, amphibian RNases, such ranpirnase and amphinase from the Northern leopard frog, escape mammalian RI and have been noted to have ...
Cyclic GMP-AMP synthase (cGAS) is a key DNA sensor capable of detecting microbial DNA and activating the adaptor protein stimulator of interferon genes (STING), leading to interferon (IFN) production and host antiviral responses. Cells exhibited reduced type I IFN production in response to cytosolic DNA in the absence of cGAS. Although the cGAS/STING-mediated DNA-sensing signal is crucial for host defense against many viruses, especially for DNA viruses, few viral components have been identified to specifically target this signaling pathway. Herpes simplex virus 1 (HSV-1) is a DNA virus that has evolved multiple strategies to evade host immune responses. In the present study, we found that HSV-1 tegument protein UL41 was involved in counteracting the cGAS/STING-mediated DNA-sensing pathway. Our results showed that wild-type (WT) HSV-1 infection could inhibit immunostimulatory DNA-induced activation of the IFN signaling pathway compared with the UL41-null mutant virus (R2621), and ectopic expression of
Ribonucleases can specifically recognize and cleave RNA at the site of sequence mismatches in RNA-DNA or RNA-RNA hybrids. The cleavage products are then characterized by gel electrophoresis. In this unit, a procedure is presented for RNase cleavage of (32)P-labeled riboprobes (transcribed from a cloned copy of the normal sequence) that have been annealed to amplified sequences of a candidate gene or cDNA obtained from affected individuals. A Support Protocol explains how to prepare riboprobes from a genomic or cDNA template obtained from a nonmutant individual. An alternate protocol describes cleavage of RNARNA hybrids using a nonisotopic RNase cleavage mutation assay. Sequential PCR and in vitro transcription steps generate sufficient quantities of duplex RNA targets so that the cleavage products can be detected on a gel by ethidium bromide staining. The unit also discusses the use of alternative ribonucleases for cleaving singlebase mismatches.
TY - JOUR. T1 - The catalytic activity and secretion of zebrafish RNases are essential for their in vivo function in motor neurons and vasculature. AU - Ferguson, Ross. AU - Holloway, Daniel E. AU - Chandrasekhar, Anand. AU - Acharya, K Ravi. AU - Subramanian, Vasanta. PY - 2019/2/1. Y1 - 2019/2/1. N2 - Angiogenin (hANG), a member of the Ribonuclease A superfamily has angiogenic, neurotrophic and neuroprotective activities. Mutations in hANG have been found in patients with Amyotrophic lateral sclerosis (ALS). The zebrafish (Danio rerio) rnasel-1, 2 and 3 are orthologues of hANG and of these only Rnasel-1 and Rnasel-2 have been shown to be angiogenic. Herein we show that NCI-65828, a potent and specific small molecule inhibitor of hANG inhibits Rnasel-1 to a similar extent. Treatment of early zebrafish embryos with NCI-65828, or with terrein, a fungal metabolite which prevents the secretion of hANG, resulted in spinal neuron aberrations as well defects in trunk vasculature. Our detailed ...
The Ribonuclease A Superfamily is composed of a group of structurally similar peptides that are secreted by immune cells and epithelial tissues. Several members of the Ribonuclease A Superfamily demonstrate antimicrobial activity, and it has been suggested that some of these ribonucleases play an essential role in host defense. Ribonuclease 7 (RNase 7) is an epithelial-derived secreted peptide with potent broad-spectrum antimicrobial activity. This review summarizes the published literature on RNase 7s antimicrobial properties, structure, regulation, and contributions to host defense. In doing so, we conclude by highlighting key knowledge gaps that must be investigated to completely understand the potential of developing RNase 7 as a novel therapeutic for human infectious diseases.
The virion host shutoff protein (Vhs) is a herpes simplex virus (HSV) protein involved in early shutoff of the host cell. It is a component of the infecting virion, located in the tegument region, that works by rapidly ...
Herpes simplex virus 1 (HSV-1) induces a profound host shut-off during lytic infection. The virion host shut-off (vhs) protein plays a key role in this process by efficiently cleaving host and viral mRNAs. Furthermore, the onset of viral DNA replication is accompanied by a rapid decline in host transcriptional activity. To dissect relative contributions of both mechanisms and elucidate gene-specific host transcriptional responses throughout the first 8h of lytic HSV-1 infection, we employed RNA-seq of total, newly transcribed (4sU-labelled) and chromatin-associated RNA in wild-type (WT) and Δvhs infection of primary human fibroblasts. Following virus entry, vhs activity rapidly plateaued at an elimination rate of around 30% of cellular mRNAs per hour until 8h p.i. In parallel, host transcriptional activity dropped to 10-20%. While the combined effects of both phenomena dominated infection-induced changes in total RNA, extensive gene-specific transcriptional regulation was observable in ...
Ribonuclease Rnase Z complexed with transfer RNA (ribonucleic acid). Computer model showing the structure of bacterial ribonuclease Rnase Z (orange) complexed with synthetic transfer RNA (cyan). From Bacillus subtilis. - Stock Image C035/8314
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.
Fingerprint Dive into the research topics of Covalent linkage of ribonuclease S-peptide to microinjected proteins causes their intracellular degradation to be enhanced during serum withdrawal. Together they form a unique fingerprint. ...
The new understanding could help both approaches, says UW-Madison professor of biochemistry Ronald Raines, who has long studied ribonucleases - enzymes that break apart RNA, a messenger with multiple roles inside the cell. In 1998, he discovered how to alter one ribonuclease to avoid its deactivation in the body. Soon thereafter, he found that the engineered ribonuclease was more toxic to cancer cells than to others.. Raines patented the advance through the Wisconsin Alumni Research Foundation and with UW-Madison chemist Laura Kiessling cofounded Quintessence Biosciences in Madison. They remain shareholders in the firm, which has licensed the patent from WARF and begun early-phase human trials with the ribonuclease at the UW Carbone Cancer Center and MD Anderson Cancer Center in Houston.. The current study began as an effort to figure out why the ribonuclease was selective for cancer cells. To identify which structure on the cell surface helped it enter the cell, Raines screened 264 structures ...
The new understanding could help both approaches, says UW-Madison professor of biochemistry Ronald Raines, who has long studied ribonucleases - enzymes that break apart RNA, a messenger with multiple roles inside the cell. In 1998, he discovered how to alter one ribonuclease to avoid its deactivation in the body. Soon thereafter, he found that the engineered ribonuclease was more toxic to cancer cells than to others.. Raines patented the advance through the Wisconsin Alumni Research Foundation and with UW-Madison chemist Laura Kiessling cofounded Quintessence Biosciences in Madison. They remain shareholders in the firm, which has licensed the patent from WARF and begun early-phase human trials with the ribonuclease at the UW Carbone Cancer Center and MD Anderson Cancer Center in Houston.. The current study began as an effort to figure out why the ribonuclease was selective for cancer cells. To identify which structure on the cell surface helped it enter the cell, Raines screened 264 structures ...
X-ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity. - Jozef Sevcik, Lubica Urbanikova, Peter A Leland, Ronald T Raines
CP000859.PE14 Location/Qualifiers FT CDS_pept 15398..16750 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Dole_0014 FT /product=putative ribonuclease BN FT /note=TIGRFAM: putative ribonuclease BN; PFAM: FT ribonuclease BN; KEGG: pin:Ping_1819 putative ribonuclease FT BN FT /db_xref=EnsemblGenomes-Gn:Dole_0014 FT /db_xref=EnsemblGenomes-Tr:ABW65824 FT /db_xref=GOA:A8ZRQ7 FT /db_xref=InterPro:IPR017039 FT /db_xref=InterPro:IPR036388 FT /db_xref=InterPro:IPR036390 FT /db_xref=UniProtKB/TrEMBL:A8ZRQ7 FT /protein_id=ABW65824.1 FT /translation=MNESKKKRLAARTSGALDFLRTGIWRVRLRELETRERVLVRYARI FT FMIAGREFITDGGPLRASALTFYTVLSLVPVMALAFAVAKGFGLQQTLEKEVLAQFPGQ FT EAVILQMIEYARALLDQTKGGLLAGVGVAVLIWTVIKVLNNIEKSFNAIWANTTPRSMG FT KKFSDYLSIMLVGPLLLILSGSATVLVATQVTAITNKIFFLGWFAPIIMTGLQLLPYLF FT VWLLFSFIYGFMPNTRVPVRSCIFGGVLAGTAFKLLQWAYLIFQVGVSRYNAIYGSFAA FT LPLFLIWMQLSWLVTLFGAELAYAHQSVGHYELEPDSRNISDFLKRIYGLYVAHLLVKT FT FKNGEPPLTADQISARLDLPIRMVNRLLETLSAAGLATQTLSGTGGDPAWQPGRDITDI FT ...
Ribonuclease - Instruments Consumables Reagents Advanced BioMatrix,RANDOX,RANDOX ELISA,Biomedical, biochemical reagents, laboratory supplies, equipment, antibodies, ELISA kits, diagnostic reagents, methods of experimental techniques, general analytical instruments, material testing instruments and equipment, used laboratory equipment, instruments and equipment, life sciences, environmental monitoring equipment , measurement, measuring instruments, rotating wall bioreactor, three-dimensional tissue / stem cell culture system; microcapsule
NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Related Articles NMR study of the cold, heat, and pressure unfolding of
Buy our Natural cow Ribonuclease A protein. Ab52579 is an active full length protein produced in Nativesyntheticaly and has been validated in ChIP. Abcam…
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
RNases are an often feared in molecular biology labs because of their high stability and ominous presence in virtually all living systems. Consequently, people who work with RNA are trained to exercise extreme caution to avoid RNA degradation: change gloves often because human hands ooze RNases; use only sterilized labware as microbes may be sources of RNases; for surfaces that cant be autoclaved, use sprays like RNase Zap (SDS- or guanidine-containing solutions). Such cautionary steps are especially necessary when dealing with low abundance RNA samples.. RNAs can be produced by in vitro transcription (IVT), a simple reaction requiring only a DNA template (double-stranded or even single-stranded DNA as long as the promoter region is double-stranded), RNA polymerase (from T7, SP6, or T3 phage), NTPs, and a reaction buffer that provides appropriate salt and pH. Standard NTPs may be replaced with modified ones to either increase stability or to reduce immune-response when transfected into ...
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Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential ...
RIBONUCLEASE A FAMILY, 1 (Ribonuclease pancreatic) is an enzyme that in humans is encoded by the RNASE1 gene. By genomic sequence analysis, RNASE1…
We characterized the activity of Barnase on an inducible plasmid constructed by UC Berkeley for iGEM 2007 (part I716408C). This construct works by expressing background levels of Barstar with in the presence of an inducible Barnase. When induced, Barnase will overwhelm Barstar. Higher levels of Barnase expression resulted in lower rates of growth in the bacteria, affirming the principle of Barnase-based growth control for the genetic fence, and confirming the results from Berkeley 2008. We characterized the growth repression of Barnase under a range of arabinose inducer concentrations ...
Complete information for RNY1 gene (RNA Gene), RNA, Ro-Associated Y1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for RNY5 gene (RNA Gene), RNA, Ro-Associated Y5, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
1AFK: Crystal structures of ribonuclease A complexes with 5-diphosphoadenosine 3-phosphate and 5-diphosphoadenosine 2-phosphate at 1.7 A resolution.
These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
MPGGGSQEYGVLCIQEYRKNSKVESSTRNNFMGLKDHLGHDLGHLYVESTDPQLSPAVPWSTVENPSMDT 1 - 70 VNVGKDEKEASEENASSGDSEENTNSDHESEQLGSISVEPGLITKTHRQLCRSPCLEPHILKRNEILQDF 71 - 140 KPEESQTTSKEAKKPPDVVREYQTKLEFALKLGYSEEQVQLVLNKLGTDALINDILGELVKLGNKSEADQ 141 - 210 TVSTINTITRETSSLESQRSESPMQEIVTDDGENLRPIVIDGSNVAMSHGNKEVFSCRGIKLAVDWFLER 211 - 280 GHKDITVFVPAWRKEQSRPDALITDQEILRKLEKEKILVFTPSRRVQGRRVVCYDDRFIVKLAFESDGII 281 - 350 VSNDNYRDLANEKPEWKKFIDERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPIVPEHKKQPCPYGK 351 - 420 KCTYGHKCKYYHPERGSQPQRSVADELRAMSRNTAAKTANEGGLVKSNSVPCSTKADSTSDVKRGAPKRQ 421 - 490 SDPSIRTQVYQDLEEKLPTKNKLETRSVPSLVSIPATSTAKPQSTTSLSNGLPSGVHFPPQDQRPQGQYP 491 - 560 SMMMATKNHGTPMPYEQYPKCDSPVDIGYYSMLNAYSNLSLSGPRSPERRFSLDTDYRISSVASDCSSEG 561 - 630 SMSCGSSDSYVGYNDRSYVSSPDPQLEENLKCQHMHPHSRLNPQPFLQNFHDPLTRGQSYSHEEPKFHHK 631 - 700 PPLPHLALHLPHSAVGARSSCPGDYPSPPSSAHSKAPHLGRSLVATRIDSISDSRLYDSSPSRQRKPYSR 701 - 770 QEGLGSWERPGYGIDAYGYRQTYSLPDNSTQPCYEQFTFQSLPEQQEPAWRIPYCGMPQDPPRYQDNREK 771 - 840 ...
pep:known chromosome:VEGA66:14:44102654:44103534:1 gene:OTTMUSG00000034641 transcript:OTTMUST00000087933 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Ear2 description:eosinophil-associated, ribonuclease A family, member 2 ...
pep:known chromosome:VEGA66:14:51853768:51854643:1 gene:OTTMUSG00000036430 transcript:OTTMUST00000093341 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Ear6 description:eosinophil-associated, ribonuclease A family, member 6 ...
Dielo spisovateľky Jany Juráňovej - próza Nevybavená záležitosť (ASPEKT 2013) zrkadlí v útržkoch minulosti súčasnosť a vice versa. Nevybavená záležitosť sa dostala do tohtoročnej finálovej desiatky Ceny J. Johanidesa.
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Paracoccidioidomycosis is a chronic granulomatous disease caused by the fungus Paracoccidioides brasiliensis. Although eosinophils have long been associated with the immune defense against helminths, the role of eosinophils in the immune response to fungal diseases is not as well studied. The eosinophil granule major basic protein is toxic to helminths and mammalian cells in vitro, and its release has been used as a marker of eosinophil localization and degranulation. To determine whether eosinophil infiltration and degranulation, as evidenced by the deposition of major basic protein, occur in lesions of P. brasiliensis, we used an immunofluorescence technique to localize the P. brasiliensis organisms and eosinophils and major basic protein. Initially, all tissues were stained with polyclonal antibody to major basic protein; subsequently, colocalization of major basic protein and P. brasiliensis by double staining with mouse and rabbit antibodies, respectively, was performed. Nine biopsy tissues from
PRG2 antibody [1.B.787] (proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)) for ELISA, IHC-Fr, IHC-P, WB. Anti-PRG2 mAb (GTX14462) is tested in Human samples. 100% Ab-Assurance.
TY - JOUR. T1 - The 5′-termini of the oligonucleotides from ribonuclease T1 digested E. coli ribosomes. AU - Lee, J. C.. AU - Quintanilla, I. V.. PY - 1973/3/5. Y1 - 1973/3/5. N2 - Oligonucleotides remaining in the 70s Escherichia coli ribosomal particles after varying degrees of digestion with ribonuclease T1 were phosphorylated with polynucleotide kinase in the presence of γ-labeled32P-ATP. The resulting radioactively labeled RNA molecules were further digested with pancreatic ribonuclease and analyzed by a two-dimensional finger-printing technique. The numbers of labeled oligonucleotides were proportional to the duration of T1 digestion; most of these oligonucleotides yielded *pAp and/or *pCp as their 5′-end groups upon alkaline hydrolysis.. AB - Oligonucleotides remaining in the 70s Escherichia coli ribosomal particles after varying degrees of digestion with ribonuclease T1 were phosphorylated with polynucleotide kinase in the presence of γ-labeled32P-ATP. The resulting radioactively ...
TY - JOUR. T1 - Preparation and properties of water-insoluble derivatives of ribonuclease T1. AU - Lee, J. C.. N1 - Funding Information: The author wishes to thank Professor V. M. Ingram for his interest and for the use of his laboratory during the initial phase of this investigation. The support by the U.S. Public Health Service (grant No. AM o839 o) is acknowledged.. PY - 1971/6/16. Y1 - 1971/6/16. N2 - Several enzymatically active water-insoluble ribonuclease T1 (ribonucleate guaninenucleotide-2′-transferase (cyclizing), EC 2.7.7.26) derivatives were prepared. One of these, Sepharose T1, which was prepared by chemically coupling ribonuclease T1 to Sepharose, was further characterized. The enzyme derivative was stable and had no detectable residual soluble enzymatic activity. Substrate specificity of the enzyme derivative remained unaltered. Kinetic values were similar to the free, native enzyme.. AB - Several enzymatically active water-insoluble ribonuclease T1 (ribonucleate ...
1. U.v. difference spectra show that the anionic surfactant sodium n-dodecyl sulphate unfolds ribonuclease A at pH7.3 and 10.3, but that the cationic surfactant n-dodecyltrimethylammonium bromide does not affect the conformation of the enzyme. 2. Equilibrium-dialysis experiments show that sodium n-dodecyl sulphate binds to ribonuclease A, but no binding of n-dodecyltrimethylammonium bromide could be detected at pH7.3. 3. The enzymic activity of ribonuclease A is unaffected by n-dodecyltrimethylammonium bromide up to a concentration of 0.03m at 25°C. 4. Ultracentrifuge studies support the conclusion that n-dodecyltrimethylammonium bromide does not interact significantly with ribonuclease A. 5. The enthalpy change as measured by microcalorimetry on binding of sodium n-dodecyl sulphate to ribonuclease A is consistent with an exothermic enthalpy of binding occurring simultaneously with an endothermic enthalpy of chain unfolding.. ...
Ribonuclease III (RNase III or RNase C)(BRENDA 3.1.26.3) is a type of ribonuclease that recognizes dsRNA and cleaves it at specific targeted locations to transform them into mature RNAs. These enzymes are a group of endoribonucleases that are characterized by their ribonuclease domain, which is labelled the RNase III domain. They are ubiquitous compounds in the cell and play a major role in pathways such as RNA precursor synthesis, RNA Silencing, and the pnp autoregulatory mechanism. Within the RNase III superfamily, there are four known classes: 1, 2, 3, and 4. Each class is defined by its structural difference. Class 1 RNase III Class 1 RNase III have a dimer structure whose function is to cleave dsRNA into multiple subunits. It is a Mg2+ dependent endonuclease and is largely found in bacteria and bacteriophage. Recently, class 1 RNase III was found in Glomeromycotan Fungi, which was suspected to be the result of horizontal gene transfer from cyanobacteria . Among the RNases III in the class ...
The isolation and characterization of the initial intermediates formed during the irreversible acid denaturation of enzyme Ribonuclease A are described. The products obtained when RNase A is maintained in 0.5 M HCl at 30° for periods up to 20 h have been analyzed by ion-exchange chromatography on Amberlite XE-64. Four distinct components were found to elute earlier to RNase A; these have been designated RNase Aa2, Aa1c, Aa1b, and Aa1a in order of their elution. With the exception of RNase Aa2, the other components are nearly as active as RNase A. Polyacrylamide gel electrophoresis at near-neutral pH indicated that RNase Aa1a, Aa1b, and Aa1c are monodeamidated derivatives of RNase A; RNase Aa2 contains, in addition, a small amount of a dideamidated component. RNase Aa2, which has 75% enzymic activity as compared to RNase A, consists of dideamidated and higher deamidated derivatives of RNase A. Except for differences in the proteolytic susceptibilities at an elevated temperature or acidic pH, the ...
Degradation of mRNA is a highly regulated step important for proper gene expression. Degradation of eukaryotic mRNA is initiated by shortening of the 3 end located poly(A) tail. Poly(A)-specific ribonuclease (PARN) is an oligomeric enzyme that degrades the poly(A) tail with high processivity. A unique property of PARN is its ability to interact not only with the poly(A) tail but also with the 5 end located mRNA cap structure. A regulatory role in protein synthesis has been proposed for PARN based on its ability to bind the cap that is required for efficient initiation of eukaryotic mRNA translation. Here we have investigated how the cap structure influences PARN activity and how PARN binds the cap. We show that the cap activates PARN and enhances the processivity of PARN. Further we show that the cap binding complex (CBC) inhibits PARN activity through a protein-protein interaction. To investigate the cap binding property of PARN, we identified the cap binding site at the molecular level using ...
TY - JOUR. T1 - Antitumor activity and toxicity of anti-HER2 immunoRNase scFv 4D5-dibarnase in mice bearing human breast cancer xenografts. AU - Balandin, Taras G.. AU - Edelweiss, Evelina. AU - Andronova, Natalia V.. AU - Treshalina, Elena M.. AU - Sapozhnikov, Alexander M.. AU - Deyev, Sergey M.. PY - 2011/2. Y1 - 2011/2. N2 - Summary: Ribonucleases (RNases) are a non-mutagenic alternative to harmful DNA-damaging anticancer drugs. Targeting of RNases with antibodies to surface antigens that are selectively expressed on tumor cells endows specificity to the cytotoxic actions of RNases. Barnase, a ribonuclease from Bacillus amyloliquefaciens, is a promising candidate for targeted delivery to cancer cells because of its insusceptibility to the ubiquitous cytoplasmic ribonuclease inhibitor, and its high stability and catalytic activity. Here, we characterized in vitro and in vivo an immunoRNase, scFv 4D5-dibarnase, which consists of two barnase molecules that are fused serially to the single-chain ...
Ribonuclease bound to transfer RNA. Computer model showing the molecular structure of a ribonuclease Z (RNase Z, blue) enzyme bound to a transfer RNA (tRNA) molecule (red). RNase is a type of nuclease that catalyses the degradation of RNA (ribonucleic acid) into smaller components in preparation for other genetic processes. tRNA is RNA that transfers a specific active amino acid to a growing polypeptide chain at the site of protein synthesis during gene translation. RNase Z causes conformational changes in both molecules to promote reorganization of the catalytic site and tRNA cleavage. - Stock Image C008/8444
In this study, we evaluated nine laboratory buffers and water samples to assess the level of RNase contamination present in a RNase-free laboratory. We also assessed the ability of Recombinant RNasin Ribonuclease Inhibitor to protect RNA in all of the sampled water and buffers. In the samples that were contaminated to some degree with RNases, Recombinant RNasin Inhibitor was able to protect introduced RNA from degradation.
Fingerprint Dive into the research topics of Mouse eosinophil-associated ribonucleases: A unique subfamily expressed during hematopoiesis. Together they form a unique fingerprint. ...
Other articles where Barnase is discussed: bacillus: … encoding an enzyme known as barnase in B. amyloliquefaciens is of interest in the development of genetically modified (GM) plants. Barnase combined with another protein synthesized by B. amyloliquefaciens known as barstar, forming the barnase-barstar gene system, was used to develop a line of non-self-fertilizing transgenic mustard (Brassica juncea) plants…
The circular-dichroism and proton-magnetic-resonance spectra of complexes of ribonuclease A with dihydrouridine 3′-phosphate, 2′- and 3′-CMP, arabinosyl-3′-CMP, 1-(2-hydroxyethyl)cytosine 2′-phosphate and 1-(3-hydroxypropyl)cytosine 3′-phosphate were studied. Comparison of the results shows that non-additivity of the circular-dichroic spectrum of an enzyme-nucleotide complex may be due to: (a), alteration of the circular dichroic spectrum of the nucleotide under the influence of the asymmetric protein matrix (induced dichroism), and (b) a change in the nucleotide conformation. The contribution of each of the two factors was estimated to calculate the circular-dichoroic spectra of 2′-CMP and 3′-CMP in complex with ribonuclease A. 3′-CMP in this complex was characterized by negative circular dichroism in the long-wavelength absorption band of the nucleotide, whereas 2′-CMP was characterized by positive circular dichroism. Since both nucleotides in the complex are known to be in ...
The circular-dichroism and proton-magnetic-resonance spectra of complexes of ribonuclease A with dihydrouridine 3′-phosphate, 2′- and 3′-CMP, arabinosyl-3′-CMP, 1-(2-hydroxyethyl)cytosine 2′-phosphate and 1-(3-hydroxypropyl)cytosine 3′-phosphate were studied. Comparison of the results shows that non-additivity of the circular-dichroic spectrum of an enzyme-nucleotide complex may be due to: (a), alteration of the circular dichroic spectrum of the nucleotide under the influence of the asymmetric protein matrix (induced dichroism), and (b) a change in the nucleotide conformation. The contribution of each of the two factors was estimated to calculate the circular-dichoroic spectra of 2′-CMP and 3′-CMP in complex with ribonuclease A. 3′-CMP in this complex was characterized by negative circular dichroism in the long-wavelength absorption band of the nucleotide, whereas 2′-CMP was characterized by positive circular dichroism. Since both nucleotides in the complex are known to be in ...
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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Nocturnin (NOCT) is a rhythmically expressed protein that regulates metabolism under the control of circadian clock. It has been proposed that NOCT deadenylates and regulates metabolic enzyme mRNAs. However, in contrast to other deadenylases, purified NOCT lacks the deadenylase activity. To identify the substrate of NOCT, we conducted a mass spectrometry screen and report that NOCT specifically and directly converts the dinucleotide NADP+ into NAD+ and NADPH into NADH. Further, we demonstrate that the Drosophila NOCT ortholog, Curled, has the same enzymatic activity. We obtained the 2.7 Å crystal structure of the human NOCT•NADPH complex, which revealed that NOCT recognizes the chemically unique ribose-phosphate backbone of the metabolite, placing the 2′-terminal phosphate productively for removal. We provide evidence for NOCT targeting to mitochondria and propose that NADP(H) regulation, which takes place at least in part in mitochondria, establishes the molecular link between circadian clock and
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The 5S rRNA maturase, ribonuclease M5, is a Toprim domain family member: The maturation of 5S ribosomal RNA in low G+C Gram-positive bacteria is catalyzed by a
Specifically, the enzymes are involved in endonucleolytic cleavage of 3-phosphomononucleotides and 3-phosphooligonucleotides ending in C-P or U-P with 2,3-cyclic phos
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Other articles where Renaturation is discussed: denaturation: …subject to this process, called renaturation, include serum albumin from blood, hemoglobin (the oxygen-carrying pigment of red blood cells), and the enzyme ribonuclease. The denaturation of many proteins, such as egg white, is irreversible. A common consequence of denaturation is loss of biological activity (e.g., loss of the catalytic ability…
Enzymes are nanomachines that are exceptionally efficient at catalyzing a chemical reaction. They play a role in all cellular mechanisms. Like all proteins, they are made up of amino acid chains that are folded and assembled in a very precise 3D structure. Some enzymes, like ribonuclease A, are so efficient that they catalyze the transformation of chemical molecules thousands of times per second.. In this study, Donald Gagné, a researcher in Professor Doucets lab holding a PhD in biology from INRS, analyzed the impact of removing a methyl group located near a loop distant from the reaction site of ribonuclease A-a very slight change that presumably would have no effect. The mutation does not perturb the 3D structure of the enzyme. However, it did result in a four-fold reduction in the affinity of ribonuclease A for nucleotides (molecules to which it must bind to carry out its function). How is this possible?. Using crystallography techniques and nuclear magnetic resonance to examine the enzyme ...
N-2-Benzoyl-5-O-dimethoxytrityl-2-O-tetrahydropyranylguanosine (5) and 1-acetyl-5-bromo-4-chloroindol-3-yl-3-phosphorodichloridate (7) were synthesized and coupled to give the title compound 9.. Keywords: Identification of ribonuclease activity. ...
sample_1: Ribonuclease III, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 20 mM; sodium chloride 150 mM. sample_2: Ribonuclease III, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 100%; sodium chloride 10 mM; sodium phosphate 150 mM. sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K ...
Differential scanning calorimetry, urea denaturation, and X-ray crystallography were combined to study the structural and energetic consequences of refilling an engineered cavity in the hydrophobic core of RNase T1 with CH(3), SH, and OH groups. Three valines that cluster together in the major hydrophobic core of T1 were each replaced with Ala, Ser, Thr, and Cys. Compared to the wild-type protein, all these mutants reduce the thermodynamic stability of the enzyme considerably. The relative order of stability at all three positions is as follows: Val , Ala approximately equal to Thr , Ser. The effect of introducing a sulfhydryl group is more variable. Surprisingly, a Val --, Cys mutation in a hydrophobic environment can be as or even more destabilizing than a Val --, Ser mutation. Furthermore, our results reveal that the penalty for introducing an OH group into a hydrophobic cavity is roughly the same as the gain obtained from filling the cavity with a CH(3) group. The inverse equivalence of the ...
Ribonuclease, Ribonuclease Iii, mRNA, Ribose, RNA, RNA Cleavage, Gene, Gene Expression, Report, Distance, Family, Hydroxyl, Micrornas, miRNA, Mirnas, Pre-mirna, Rnase, Rnase Iii, Seed, Concentrations
The accessibility of methionines in RNAase A to reaction with OBQ has been studied at highly acidic pH. The differences between the rate constants of reactions of the methionine and methionines of RNAase A with OBQ is a reflection on the limited accessibility of methionines in the protein conformation. Nevertheless, at sufficiently high OBQ concentration, all the four methionines of the enzyme can be modified. At lower concentration of OBQ, a derivative may be prepared in which a specific methionine is modified. The introduced chromophore ionizes at around pH 3 in this derivative. The derivative has partial activity towards RNA which is enhanced on addition of S-protein. ...
To gain preferential access to the protein synthesis machinery and to disrupt induction of antiviral responses by infected cell many viruses block host gene expression. This blockade is called host shutoff and it is mediated by viral factors that either destroy host messenger RNAs (mRNAs) or interfere with their synthesis. Influenza A virus (IAV) encodes…
The Presto™ Midi Plasmid Kit was designed for Plasmid DNA Purification from 50-150 ml of cultured bacterial cells using an efficient plasmid midiprep system. For processing smaller volumes, the Presto™ Mini Plasmid Kit is also available. Both plasmid kits include TrueBlue Lysis Buffer (an optional color indicator) to prevent common handling errors, while ensuring efficient cell lysis and neutralization. The Presto™ Midi Plasmid Kit uses a modified alkaline lysis method and RNase treatment to obtain clear cell lysate with minimal genomic DNA/RNA contaminants. Using an efficient gravity-flow procedure, plasmid DNA in the crude lysate is bound by the plasmid midi column and the contaminants are removed with PW Buffer. The purified plasmid DNA is eluted by a high salt buffer and then precipitated with Isopropanol for desalting. The entire procedure can be completed in 80 minutes without ultracentrifuges, HPLC or other toxic reagents.. ...
The ribonuclease (RNase) molecule which takes part in the formation of enzyme-substrate complexes, was investigated to determine factors which affect the binding of various competitive inhibitors of RNase activity. The binding of inhibitory nucleotides, such as 2-cytidylic acid, by RNase was measured not only by enzyme inhibition, but also by spectral changes and dialysis equilibrium. As measured spectrophotometrically, complex formation between nucleotideAND RNase is manifested by changes in the spectral contributions from both pyrimidine and tyrosyl groups. The affinities of RNase for 2-cytidylic acid as measured by all 3 methods were in excellent agreement. As measured by dialysis equilibrium and spectral changes, only one molecule of nucleotide is bound per molecule of enzyme. Since 2-cytidylic acid is a competitive inhibitor of both catalytic actions (transferase and hydralase) of the enzyme, it may be inferred that the same catalytic site is responsible for both reactions. (Author)
Ribonuclease HII and HIII are endonucleases that specifically degrade the RNA of RNA-DNA hybrids. Proteins which belong to this family have been found in bacteria, archaea, and eukaryota.. The domain represented by this entry is found in ribonucleases HII.. ...
RNase A is an important enzyme for the removal of RNA for RNA free DNA purification reactions such as plasmid DNA purification and genomic DNA purification, RNA removal from recombinant protein preparations, Ribonuclease protection assays, mapping single-base mutations in DNA/RNA. RNase A effectively cleaves the phosphodiester bond between the 5-ribose of a ...
Ribonuclease H1, Ribonuclease H1, 5-R(*GP*GP*AP*GP*UP*GP*CP*GP*AP*CP*AP*CP*CP*UP*GP*AP*UP*UP*CP*C)-3), 5-D(*DGP*DGP*DAP*DAP*DTP*DCP*DAP*DGP*DGP*DTP*DGP*DTP*DCP*DGP*DCP*DAP*DCP*DTP*DCP*DT)-3 ...