PAP (polyadenylate polymerase) is the template-independent RNA polymerase responsible for synthesis of the 3′ poly(A) tails of mRNA. To investigate the role of proton transfer in the catalytic mechanism of PAP, the pH dependence of the steady-state kinetic parameters of yeast PAP were determined for the forward (adenyl transfer) and reverse (pyrophosphorolysis) reactions. The results indicate that productive formation of an enzyme-RNA-MgATP complex is pH independent over a broad pH range, but that formation of an active enzyme-RNA-MgPPi complex is strongly pH dependent, consistent with the production of a proton on the enzyme in the forward reaction. The pH dependence of the maximum velocity of the forward reaction suggests two protonic species are involved in enzyme catalysis. Optimal enzyme activity requires one species to be protonated and the other deprotonated. The deuterium solvent isotope effect on Vmax is also consistent with proton transfer involved in catalysis of a rate-determining ...
Treatment of perfused rabbit heart with reserpine causes a decrease of incorporation of labelled precursors into RNA species of subcellular fractions and polyamines. Ornithine decarboxylase, S-adenosylmethionine decarboxylase and cytoplasmic Mn2+-stimulated polyadenylate polymerase activities are not modified. Addition of noradrenaline to reserpine-treated perfused hearts enhances, compared with the control, the incorporation of precursor into RNA in all subcellular fractions other than the nuclear one, restores incorporation of labelled putrescine into polyamines, enhances ornithine decarboxylase and S-adenosylmethionine decarboxylase activities and causes a 12-fold increase in cytoplasmic Mn2+-dependent polyadenylate polymerase activity. After treatment with noradrenaline the increase in radioactivity was found solely in AMP after hydrolysis of microsomal RNA to nucleoside monophosphates. ...
Biochem Pharmacol. 2010 Mar 1;79(5):669-77. doi: 10.1016/j.bcp.2009.09.028. Epub 2009 Oct 6. Research Support, N.I.H., Extramural
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Polynucleotide Adenylyltransferase: An enzyme that catalyzes the synthesis of polyadenylic acid from ATP. May be due to the action of RNA polymerase (EC 2.7.7.6) or polynucleotide adenylyltransferase (EC 2.7.7.19). EC 2.7.7.19.
TY - JOUR. T1 - Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme. AU - Toh, Yukimatsu. AU - Numata, Tomoyuki. AU - Watanabe, Kazunori. AU - Takeshita, Daijiro. AU - Nureki, Osamu. AU - Tomita, Kozo. PY - 2008/7/23. Y1 - 2008/7/23. N2 - CCA-adding enzyme builds the 3′-end CCA of tRNA without a nucleic acid template. The mechanism for the maintenance of fidelity during the CCA-adding reaction remains elusive. Here, we present almost a dozen complex structures of the class I CCA-adding enzyme and tRNA mini-helices (mini-D 73 N 74 , mini-D 73 N 74 C 75 and mini-D 73 C 74 N 75 ; D 73 is a discriminator nucleotide and N is either A, G, or U). The mini-D 73 N 74 complexes adopt catalytically inactive open forms, and CTP shifts the enzymes to the active closed forms and allows N 74 to flip for CMP incorporation. In contrast, unlike the catalytically active closed form of the mini-D 73 C 74 C 75 complex, the mini-D 73 N 74 C 75 and mini-D 73 C 74 N 75 ...
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.
Cleavage factor Im (CFIm) is one of six factors necessary for correct cleavage and polyadenylation of pre-mRNAs. CFIm is composed of three different subunits of 25, 59, and 68 kDa, and it functions as a heterotetramer, with a dimer of the 25 kDa subunit binding to two of the 59 or 68 kDa subunits. The protein encoded by this gene represents the 59 kDa subunit, which can interact with the splicing factor U2 snRNP Auxiliary Factor (U2AF) 65 to link the splicing and polyadenylation complexes. [provided by RefSeq, Oct 2016 ...
PAN, a yeast poly(A) nuclease, plays an important nuclear role in the posttranscriptional maturation of mRNA poly(A) tails. The activity of this enzyme is dependent on its Pan2p and Pan3p subunits, as well as the presence of poly(A)-binding protein (Pab1p). We have identified and characterized the associated network of factors controlling the maturation of mRNA poly(A) tails in yeast and defined its relevant protein-protein interactions. Pan3p, a positive regulator of PAN activity, interacts with Pab1p, thus providing substrate specificity for this nuclease. Pab1p also regulates poly(A) tail trimming by interacting with Pbp1p, a factor that appears to negatively regulate PAN. Pan3p and Pbp1p both interact with themselves and with the C terminus of Pab1p. However, the domains required for Pan3p and Pbp1p binding on Pab1p are distinct. Single amino acid changes that disrupt Pan3p interaction with Pab1p have been identified and define a binding pocket in helices 2 and 3 of Pab1ps carboxy terminus. The
CPSF2兔多克隆抗体(ab100807)可与小鼠, 人样本反应并经IHC实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
CPSF30小鼠单克隆抗体[2202C1](ab51343)可与人样本反应并经WB, Dot实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
mRNA cleavage and polyadenylation specificity factor complex, 5-3 exonuclease activity, endoribonuclease activity, RNA binding, mRNA 3-end processing by stem-loop binding and cleavage, mRNA cleavage, mRNA polyadenylation
Complete information for TRNT1 gene (Protein Coding), TRNA Nucleotidyl Transferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for TRNT1 gene (Protein Coding), TRNA Nucleotidyl Transferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Mouse anti Human caspase-14, clone 4C9 recognizes human caspase-14, a 242 amino acid ~28 kDa non-apoptotic caspase which exists as a
Fission yeast Cid13 and budding yeast Trf4/5 are members of a newly identified nucleotidyltransferase family conserved from yeast to man. Trf4/5 are thought to be essential DNA polymerases. We report that Cid13 is a poly(A) polymerase. Unlike conventional poly(A) polymerases, which act in the nucleus and indiscriminately polyadenylate all mRNA, Cid13 is a cytoplasmic enzyme that specifically targets suc22 mRNA that encodes a subunit of ribonucleotide reductase (RNR). cid13 mutants have reduced dNTP pools and are sensitive to hydroxyurea, an RNR inhibitor. We propose that Cid13 defines a cytoplasmic form of poly(A) polymerase important for DNA replication and genome maintenance.. ...
Fig. 4. Excess GLD-1 causes premature meiotic entry. (A) gld-1(oz10gf) has a smaller proliferative zone than wild-type animals. Dissected gld-1(oz10gf) and wild-type gonad arms from animals grown at 20°C to one day past L4, stained with REC-8- and HIM-3-specific antibodies, and DAPI. Proliferative zone defined as the number of cell diameters from the DTC that are REC-8-positive with all cells at that distance also REC-8-positive. n=15 per genotype. t-test P,10-7. The oz10 allele contains a deletion in the gld-1 3′UTR, as well as a missense mutation in an amino acid conserved in some, but not all homologues (Jones and Schedl, 1995). The increased GLD-1 accumulation is probably due to the mutant 3′UTR causing increased translation (Crittenden et al., 2002). However, we cannot rule out the possibility that the missense mutation affects GLD-1 levels or GLD-1 activity. (B) gld-1(oz10gf) enhances the `Glp phenotype of glp-1(bn18) at 20°C. The graph shows the percentage of animals that have lost ...
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Reaktivität: Fledermaus, Huhn, Rind (Kuh) and more. 67 verschiedene CPSF4 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Effect of cordycepin on NF-κB activation. Levels of NF-κB protein in RAW 264.7 cells. Cells were incubated with various concentrations of cordycepin in the pr
AtCPSF30 is the only Arabidopsis protein with a degree of sequence similarity to other eukaryotic CPSF30 proteins that extends beyond the typical spacing of Cys and His residues in the CCCH zinc-finger motif, and a number of lines of evidence support the conclusion that AtCPSF30 is an authentic polyadenylation factor subunit. As is the case with its yeast counterpart (Yth1p; Barabino et al., 1997), AtCPSF30 interacts with another Arabidopsis polyadenylation subunit homolog, AtFip1(V) (Forbes et al., 2006); AtFip1(V) also interacts with poly(A) polymerase and thereby provides a conceptual link between AtCPSF30 and poly(A) polymerase. The results presented in this study show that AtCPSF30 is present in the nucleus (Fig. 2B), as would be expected of a polyadenylation factor subunit. The coimmunoprecipitation of AtCPSF30 by antibodies raised against AtCPSF100 (Fig. 2C) indicates that AtCPSF30 resides, at least in part, in a complex with another Arabidopsis polyadenylation factor subunit. AtCPSF30 is ...
1. WahleE (1991) A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell 66: 759-768.. 2. KuhnU, NemethA, MeyerS, WahleE (2003) The RNA binding domains of the nuclear poly(A)-binding protein. J Biol Chem 278: 16916-16925.. 3. KerwitzY, KuhnU, LilieH, KnothA, ScheuermannT, et al. (2003) Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA. Embo J 22: 3705-3714.. 4. KuhnU, GundelM, KnothA, KerwitzY, RudelS, et al. (2009) Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J Biol Chem 284: 22803-22814.. 5. KuhnU, WahleE (2004) Structure and function of poly(A) binding proteins. Biochim Biophys Acta 1678: 67-84.. 6. ApponiLH, LeungSW, WilliamsKR, ValentiniSR, CorbettAH, et al. (2010) Loss of nuclear poly(A)-binding protein 1 ...
In eukaryotic cells, pre-mRNAs undergo extensive processing in the nucleus prior to export. Processing is subject to a quality-control mechanism that retains improperly processed transcripts at or near sites of transcription. A poly(A) tail added by the normal 3′-processing machinery is necessary but not sufficient for export. Retention depends on the exosome. In this study, we identify the poly(A)-binding protein, Pab1, and the poly(A) nuclease, PAN, as important factors that couple 3′ processing to export. Pab1 contains a nonessential leucine-rich nuclear export signal and shuttles between the nucleus and the cytoplasm. It can exit the nucleus either as cargo of exportin 1 or bound to mRNA. Pab1 is essential but several bypass suppressors have been identified. Deletion of PAB1 from these bypass suppressor strains results in exosome-dependent retention at sites of transcription. Retention is also seen in cells lacking PAN, which Pab1 is thought to recruit and which may be responsible for ...
TY - JOUR. T1 - 7 tRNA Nucleotidyltransferase. AU - Deutscher, Murray P. PY - 1982/12/1. Y1 - 1982/12/1. UR - http://www.scopus.com/inward/record.url?scp=77956942628&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=77956942628&partnerID=8YFLogxK. U2 - 10.1016/S1874-6047(08)60279-6. DO - 10.1016/S1874-6047(08)60279-6. M3 - Article. AN - SCOPUS:77956942628. VL - 15. SP - 183. EP - 215. JO - Enzymes. JF - Enzymes. SN - 0423-2607. IS - C. ER - ...
Gametogenesis and early embryogenesis in many animal species often occur in the context of little or no new transcription. Instead, they rely on the translation of preexisting mRNAs that had been synthesized and stockpiled earlier in gametogenesis. Translation of these mRNAs must be repressed during their synthesis and deposition, and then be activated later. One mechanism to regulate the translation of maternal mRNAs is to control the length of their 3 poly(A) tails through cytoplasmic polyadenylation. Studies in C. elegans identified a cytoplasmic poly(A) polymerase (PAP) GLD-2 that, in complex with an RNA-binding protein GLD-3, extends poly(A) tails of stored maternal mRNAs during oogenesis. Here, I identified the two GLD-2 cytoplasmic PAPs in Drosophila melanogaster. Using yeast two-hybrid assays I showed that both can interact with the Drosophila GLD-3 (Bic-C). I showed that one Drosophila GLD-2 PAP is expressed in the female germline, and the other in testes. I focused my subsequent ...
Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of protein-protein interactions and gene expression profiling. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Cleavage and polyadenylation specificity factor (CPSF) is relevant to the cleavage of the 3′ signaling region from a newly synthesized pre-messenger RNA (pre-mRNA) molecule. Specifically, it is in the process…. Read More Read More. ...
Adenylic acid. Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2-, 3-, or 5-position ...
Recombinant protein from the full-length sequence of homo sapiens cleavage and polyadenylation factor I subunit 1 (CLP1), transcript variant 1 (NM_006831), with a His tag., from EUPROTEIN
Digestia începe în gurǎ, unde sfǎrâmǎm alimentele cu limba şi dinţii. Apoi particulele de mâncare trec spre stomac, unde acestea sunt în continuare di...
Emerging evidence has demonstrated that regulating the length of the poly(A) tail on an mRNA is an efficient means of controlling gene expression at the post-transcriptional level. In early development, transcription is silenced and gene expression is primarily regulated by cytoplasmic polyadenylation. In somatic cells, considerable progress has been made toward understanding the mechanisms of negative regulation by deadenylation. However, positive regulation through elongation of the poly(A) tail has not been widely studied due to the difficulty in distinguishing whether any observed increase in length is due to the synthesis of new mRNA, reduced deadenylation or cytoplasmic polyadenylation. Here, we overcame this barrier by developing a method for transcriptional pulse-chase analysis under conditions where deadenylases are suppressed. This strategy was used to show that a member of the Star family of RNA binding proteins, QKI, promotes polyadenylation when tethered to a reporter mRNA. Although
Lipins play important roles in adipogenesis, insulin sensitivity, and gene regulation, and mutations in these genes cause lipodystrophy, myoglobinuria, and inflammatory disorders. While all lipins (lipin 1, 2, and 3) act as phosphatidic acid phosphatase (PAP) enzymes, which are required for triacylglycerol (TAG) synthesis from glycerol 3-phosphate, lipin 1 has been the focus of most of the lipin-related research. In the current issue of the JCI, Zhang et al. show that while lipin 2 and 3 are expendable for the incorporation of dietary fatty acids into triglycerides, lipin 2/3 PAP activity has a critical role in phospholipid homeostasis and chylomicron assembly in enterocytes.. ...
A metal scavenging study using SiliaBond® Metal Scavengers products was conducted on Grubbs, Hoveyda-Grubbs, TPAP and RuCl3 catalysts.
The process of 3′ end formation/polyadenylation occurs co-transcriptionally on cellular and HIV mRNAs generated by RNA Pol II and influences the termination of transcription at a site several hundred bases downstream of the mature 3′ end of the mRNA [50]. The 3′ end of most human mRNAs is generated first by an endonucleolytic cleavage event (catalyzed by CPSF73, aka CPSF3) followed by the addition of 100-250 adenylate residues by poly(A) polymerase (PAP). A typical polyadenylation signal contains two types of elements. The core elements consist of an AAUAAA or similar hexanucleotide and a short (about 5 base long) U- or GU-rich tract located within approximately 25-30 bases upstream or downstream, respectively, of the site. The core elements serve as the assembly site of the complex of polyadenylation factors. Many polyadenylation signals also contain auxiliary elements that are located upstream or downstream of the core elements. These auxiliary elements bind to a variety of cellular ...
Availability of large numbers of transcriptomic sequences provides an unprecedented opportunity to explore genome-wide polyadenylation profiles. The standard RNA-seq reads are commonly used to define the genome wide polyadenylation profiles in species with no available or limited polyadenylation data (Zhao et al. 2014; Wang et al. 2016b). Here, 9.48 billion RNA-Seq reads from the 24 high-throughput transcriptomic studies were analyzed to comprehensively characterize genome-wide polyadenylation profiles in the maize. The datasets used in this study consists of 401 pooled samples collected from different tissues under various physiological and developmental conditions (Table S1). Using a robust PAC identification process (Dong et al. 2015) with slight modifications, 21 million transcriptomic reads with eight or more terminal A- or T-residues were used to find the evidence for 95,345 polyadenylation events (PACs) in the maize genome.. Heterogeneity in the polyadenylation events is a common ...
We have isolated the human homolog of S. cerevisiae Fip1p and have found that hFip1 is a genuine subunit of CPSF. Our results reported here indicate that hFip1 contributes to poly(A) site recognition and to CPSF‐dependent stimulation of polyadenylation. hFip1 binds to U‐rich sequence elements on the pre‐mRNA and is able to stimulate the activity of PAP.. CPSF has originally been described as a tetrameric complex containing the subunits CPSF160, CPSF100, CPSF73 and CPSF30, based on their stoichiometric cofractionation with CPSF activity. These polypeptides are related to four subunits of the yeast polyadenylation factor CPF (Yhh1p, Ydh1p, Ysh1p and Yth1p). However, CPF contains additional subunits (Preker et al, 1997; Dichtl et al, 2002a; Gavin et al, 2002; Walsh et al, 2002), one of which is Fip1p. Based on sequence conservation, we have identified the human homolog of yeast Fip1p and have shown that hFip1 is an additional, so far unrecognized subunit of CPSF. Most likely, hFip1 has not ...
Most eukaryotic mRNAs have a sequence of polyadenylic acid [poly(A)] at their 3-termini. Although it has been almost two decades since the discovery of these poly(A) tracts, their function(s) have yet to be clarified. Earlier results from our laboratory led us to propose that poly(A) has a role in translation. More specifically, we proposed that an interaction of the cytoplasmic poly(A)-binding protein (PABP) with a critical minimum length of poly(A) facilitates the initiation of translation of poly(A)+, but not poly(A)-, mRNAs. The results of several different experimental approaches have provided evidence which indirectly supports this hypothesis. These results include: 1) the correlation of specific changes in mRNA poly(A) tail length with translational efficiency in vivo and in vitro; 2) correlations between the abundance and stability of PABPs and the rate of translational initiation in vivo and in vitro; and 3) the demonstration that exogenous poly(A) is a potent and specific inhibitor of the in
Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3 to 5 exoribonuclease activity and a 3-terminal oligonucleotide polymerase activity.[2] That is, it dismantles the RNA chain starting at the 3 end and working toward the 5 end.[1] It also synthesizes long, highly heteropolymeric tails in vivo. It accounts for all of the observed residual polyadenylation in strains of Escherichia coli missing the normal polyadenylation enzyme.[1] Discovered by Marianne Grunberg-Manago working in Severo Ochoas lab in 1955, the RNA-polymerization activity of PNPase was initially believed to be responsible for DNA-dependent synthesis of messenger RNA, a notion that got disproved by the late 1950s.[3][4] It is involved in mRNA processing and degradation in bacteria, plants,[5] and in humans.[6] In humans, the enzyme is encoded by the PNPT1 gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two ...
This gene encodes a subunit of the Integrator complex. This protein complex binds the C-terminal domain of RNA polymerase II and likely plays a role in small nuclear RNA processing. The encoded protein has similarities to the subunits of the cleavage and polyadenylation specificity factor complex. Alternatively spliced transcript variants have been described.[provided by RefSeq, Feb 2010 ...
.. (PABP C1) non-polymorphisms mRNA poly(A) tails Polyadenylation in vivo and Exons correlate with the centromere cells is made from its zymogen the C1-complex shows that the abundance for the effect of excess cellular poly(A)-PABP transfection of p53 and loss of p53-mediated control over c-myc-dependent transactivation. Whether factor 4E (eIF4E). Exposure of human cell…