Peptide Elongation Factor Tu: A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.Peptide Elongation Factor 1: Peptide elongation factor 1 is a multisubunit protein that is responsible for the GTP-dependent binding of aminoacyl-tRNAs to eukaryotic ribosomes. The alpha subunit (EF-1alpha) binds aminoacyl-tRNA and transfers it to the ribosome in a process linked to GTP hydrolysis. The beta and delta subunits (EF-1beta, EF-1delta) are involved in exchanging GDP for GTP. The gamma subunit (EF-1gamma) is a structural component.Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.GTP Phosphohydrolase-Linked Elongation Factors: Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.Peptide Chain Elongation, Translational: A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.Peptide Elongation Factor 2: Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.Peptide Elongation Factor G: Peptide Elongation Factor G catalyzes the translocation of peptidyl-tRNA from the A to the P site of bacterial ribosomes by a process linked to hydrolysis of GTP to GDP.Poly U: A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Pyridones: Pyridine derivatives with one or more keto groups on the ring.RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.Aurodox: Antibiotic obtained from a Streptomyces variant considered as possibly effective against Streptococcus pyogenes infections. It may promote growth in poultry.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Peptide Biosynthesis: The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.Transcriptional Elongation Factors: Transcription factors whose primary function is to regulate the rate in which RNA is transcribed.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Guanine NucleotidesElongation Factor 2 Kinase: A monomeric calcium-calmodulin-dependent protein kinase subtype that specifically phosphorylates PEPTIDE ELONGATION FACTOR 2. The enzyme lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE, however it is regulated by phosphorylation by PROTEIN KINASE A and through intramolecular autophosphorylation.Thermus thermophilus: A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Thermus: Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Tosylphenylalanyl Chloromethyl Ketone: An inhibitor of Serine Endopeptidases. Acts as alkylating agent and is known to interfere with the translation process.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Kinetics: The rate dynamics in chemical or physical systems.Bacterial Proteins: Proteins found in any species of bacterium.Peptides, Cyclic: Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.RNA, Transfer, Amino Acid-Specific: A group of transfer RNAs which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis.Positive Transcriptional Elongation Factor B: A transcriptional elongation factor complex that is comprised of a heterodimer of CYCLIN-DEPENDENT KINASE 9 and one of several CYCLINS including TYPE T CYCLINS and cyclin K. It functions by phosphorylating the carboxy-terminal domain of RNA POLYMERASE II.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Euglena gracilis: A species of fresh-water, flagellated EUKARYOTES in the phylum EUGLENIDA.Peptide Library: A collection of cloned peptides, or chemically synthesized peptides, frequently consisting of all possible combinations of amino acids making up an n-amino acid peptide.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Transfer RNA Aminoacylation: The conversion of uncharged TRANSFER RNA to AMINO ACYL TRNA.Antimicrobial Cationic Peptides: Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Ribosomal Proteins: Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.RNA, Transfer, Ala: A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Asn: A transfer RNA which is specific for carrying asparagine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Thr: A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.Anti-Bacterial Agents: Substances that reduce the growth or reproduction of BACTERIA.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.RNA Polymerase II: A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin. EC 2.7.7.6.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Transcription Factors, General: Transcription factors that form transcription initiation complexes on DNA, bind to specific DNA-DIRECTED RNA POLYMERASES and are required to initiate transcription. Although their binding may be localized to distinct sequence and structural motifs within the DNA they are considered non-specific with regard to the specific gene being transcribed.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).RNA, Transfer, Asp: A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.Guanosine Tetraphosphate: Guanosine 5'-diphosphate 2'(3')-diphosphate. A guanine nucleotide containing four phosphate groups. Two phosphate groups are esterified to the sugar moiety in the 5' position and the other two in the 2' or 3' position. This nucleotide serves as a messenger to turn off the synthesis of ribosomal RNA when amino acids are not available for protein synthesis. Synonym: magic spot I.Fusidic Acid: An antibiotic isolated from the fermentation broth of Fusidium coccineum. (From Merck Index, 11th ed). It acts by inhibiting translocation during protein synthesis.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Oligopeptides: Peptides composed of between two and twelve amino acids.Genes, Bacterial: The functional hereditary units of BACTERIA.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Aminoglycosides: Glycosylated compounds in which there is an amino substituent on the glycoside. Some of them are clinically important ANTIBIOTICS.Geobacillus stearothermophilus: A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Guanylyl Imidodiphosphate: A non-hydrolyzable analog of GTP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It binds tightly to G-protein in the presence of Mg2+. The nucleotide is a potent stimulator of ADENYLYL CYCLASES.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Histidine: An essential amino acid that is required for the production of HISTAMINE.Molecular Weight: The sum of the weight of all the atoms in a molecule.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Natriuretic Peptide, Brain: A PEPTIDE that is secreted by the BRAIN and the HEART ATRIA, stored mainly in cardiac ventricular MYOCARDIUM. It can cause NATRIURESIS; DIURESIS; VASODILATION; and inhibits secretion of RENIN and ALDOSTERONE. It improves heart function. It contains 32 AMINO ACIDS.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
Rao TR, Slobin LI (Mar 1986). "Structure of the amino-terminal end of mammalian elongation factor Tu". Nucleic Acids Research. ... "Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431 ... It is postulated that high expression and secretion of elongation factors from tumor tissues, combined with altered levels of ... eEF1A-derived bacterial peptides in neoplastic disease, may lead to autoimmunity in breast cancer. As with breast cancer, ...
Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S (March 1999). "A novel ubiquitination factor, E4, is involved in ... E4 enzymes, or ubiquitin-chain elongation factors, are capable of adding pre-formed polyubiquitin chains to substrate proteins ... A frameshift mutation in ubiquitin B can result in a truncated peptide missing the C-terminal glycine. This abnormal peptide, ... Once inside, the proteins are rapidly degraded into small peptides (usually 3-25 amino acid residues in length). Ubiquitin ...
Elongation factor. Prokaryotic. *EF-Tu. *EF-Ts. *EF-G. Archaeal. *aEF-1 ... Although catalysis of the peptide bond involves the C2 hydroxyl of RNA's P-site adenosine in a proton shuttle mechanism, other ... "A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress". Cell. 151 ... Elongation Factors. *Palade. *3D electron microscopy structures of ribosomes at the EM Data Bank(EMDB) ...
EF-Tu). Upon binding of their cognate ligands, the aforementioned RLKs activate generic immune responses termed pattern ... EF-Tu). Upon binding of their cognate ligands, the aforementioned RLKs activate generic immune responses termed pattern ... and the PRR AtEFR recognizes elf18 from elongation factor ( ... and the PRR AtEFR recognizes elf18 from elongation factor ( ... EF-Tu Receptor. EF-Tu receptor is a LRR-RLK that recognizes the peptide elf18 from bacterial elongation factor (EF)-Tu. EFR and ...
2013b), we failed to detect actin remodeling after treatment with a peptide mimic of the bacterial elongation factor EF-Tu, ... These include reduction in filament disassembly via inhibition of actin depolymerizing factors (ADF4 or ADF1; Henty-Ridilla et ... including plant cell wall fragments released by pathogen lytic enzymes or peptides synthesized de novo during pathogen ... a peptide mimic of bacterial elongation factor-Tu) but is not required for chitin signaling, whereas CP and ADF1 are implicated ...
EF-Tu can traffic to and is retained on, cell surfaces where can interact with membrane receptors and with extracellular matrix ... EF-Tu can traffic to, and is retained on, cell surfaces where can interact with membrane receptors and with extracellular ... However, EF-Tu has evolved the capacity to execute diverse functions on the extracellular surface of both eukaryote and ... However, EF-Tu has evolved the capacity to execute diverse functions on the extracellular surface of both eukaryote and ...
... and translation elongation factor Tu; all of these are released from bacterial pathogens (Nürnberger et al., 2004; Boller and ... the WRKY transcription factors may play an important role in the amplification of the Pep peptide signal. ... Bacterial flagellin and translation elongation factor Tu are perceived by leucine-rich repeat receptor-like kinases (LRR-RLKs) ... 2008). Structure-activity studies of AtPep1, a plant peptide signal involved in the innate immune response. Peptides 29: 2083- ...
Peptide elongation factors , Codons , Transfer RNA , EF-TU , ELONGATION-FACTOR TU , COMPLEX , PROTEIN , AMINOACYL-TRANSFER-RNA ... Peptides , Arabidopsis , Bacterial proteins , Analysis , Genetic aspects , Structure ... Peptide Elongation Factor Tu - chemistry , Cysteine - chemistry , Peptide Elongation Factor Tu - metabolism , Peptide ... Peptide Elongation Factor Tu - chemistry , Peptide Elongation Factor Tu - metabolism , Prolyl Hydroxylases - chemistry , X-Ray ...
... the elongation factors EF-G, EF-P, EF-Ts and EF-Tu, the peptide chain release factor RF1, the recycling factor RRF, the back ... that subsequently removes the formyl group from the N-terminal methionine of translated peptides, are both absent in the six ... the same enzymes that phosphorylate elongation factor EF-Tu. PrkC and PrpC are present in all members of the Spiroplasma and ... 2011) Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations. Proc Natl Acad Sci U S A ...
Other elongation factors and transcription factors were also influenced when EF-1β was suppressed. The results demonstrate ... To investigate the nature and function of elongation factor 1β from Spodoptera exigua (SeEF-1β), its cDNA was cloned. This ... is a key regulation factor for translation in many organisms, including plants, bacteria, fungi, animals and insects. ... Elongation factor is a highly conserved protein that plays a role in peptide elongation during translation [1-4] and is ...
... and the selection of cognate aminoacyl-tRNAs by the ribosome in cooperation with the GTPase elongation factor EF-Tu. These two ... Peptides Medicine & Life Sciences * Transfer RNA Aminoacylation Medicine & Life Sciences * Amino Acids Medicine & Life Sciences ... and the selection of cognate aminoacyl-tRNAs by the ribosome in cooperation with the GTPase elongation factor EF-Tu. These two ... and the selection of cognate aminoacyl-tRNAs by the ribosome in cooperation with the GTPase elongation factor EF-Tu. These two ...
Two ORFs for the elongation factor EF-G as well as EF-Tu, EF-Ts, and EF-p (elongation factor for peptide bond synthesis) genes ... T. senegalensis encodes three peptide chain release factors, RF-1, RF-2 and RF-3. Large and small ribosomal subunit proteins ... Signal peptides and numbers of transmembrane helices were predicted using SignalP [40] and TMHMM [41] respectively. ORFans were ... For transcription termination, one gene encodes a Rho factor similar to that of S. keddieii. In addition, homologs of NusA and ...
In spite of their ribosomal origin, these highly posttranslationally processed peptides have posed a fascinating synthetic ... or thiazolyl peptides, are a relatively new family of antibiotics that already counts with more than one hundred different ... bind to elongation factor Tu (EF-Tu), blocking its tRNA/amino acyl complex binding site [96,97,98]. As a consequence, the ... In the precursor peptide sequence, the structural peptide is numbered with positive figures and the leading peptide with ...
Eukaryotic Translation Elongation Factor 1 Alpha 2, including: function, proteins, disorders, pathways, orthologs, and ... Elongation factor Tu, C-terminal ProtoNet:. * Q05639 Suggested Antigen Peptide Sequences for EEF1A2 Gene. ... Binding Sites for Transcription Factors within promoters. ENSR00000139913. 215. 601. TBP GTF2F1 ZSCAN5A CTCF MXI1 ZNF146 RB1 ... No data available for DME Specific Peptides for EEF1A2 Gene Domains & Families for EEF1A2 Gene Gene Families for EEF1A2 Gene. ...
Finally, the chloroplast translation elongation factor EF-Tu (type-3 protein no. 50 in Table VII) was found to specifically ... EF-Tu is encoded by a nuclear gene in a precursor form containing an N-terminal transit peptide for plastid localization ( ... Coverage of the protein by the matching peptides must reach a minimum of 12% and at least four independent peptides should ... It is interesting that three cytosolic translation factors, numbers 105, 127, and 129, were already present from the dry mature ...
... the positions of residues that are homologous to corresponding residues of bacterial elongation factor Tu (EF-Tu) to which p21 ... For the stretch of amino acid residues 61-65, the temperature factors of backbone atoms are four times the average value of ... Pro or Gly residues to conform to standard amino acid geometry and to form trans-planar peptide bonds. Since no alpha-carbon ... Empirical Conformational Energies for Peptides Program). In Stage 2, ...
GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs. Proc. Natl. Acad. Sci. U.S.A. 92, 1945- ... EF-Tu, initiation factors, [3H]Met-tRNAfMet, f[3H]Met-tRNAfMet, and BODIPY-[3H]Met-tRNAfMet were prepared from E. coli as ... 4C). Addition of EF-Tu-GTP-Leu-tRNALeu, which leads to Leu incorporation into the nascent peptide and the next round of ... Products were separated by Tris-Tricine gel electrophoresis (36). Fluorescent peptides were detected after gel electrophoresis ...
Compared to those in adjacent normal epitheliums, the expression of 15 proteins including enolase, elongation factor Tu, ... A multiplexed, label-free multiple reaction monitoring (MRM) assay was established to target peptides specific to all detected ... Proteomic analysis identified interactions of RIOK3 with actin and several actin-binding factors including tropomyosins (TPM3 ... Proteins that exhibited significantly different expressions were identified by peptide mass fingerprinting and validated by ...
prokaryotic initiation factor 2*peptide elongation factor tu*pasteurellaceae*collectins*murine leukemia virus*cyclic amp ... gtp phosphohydrolase linked elongation factors*pentosyltransferases*peptide elongation factors*haemophilus*acyl coa ... Similar to the previously reported peptides from retro and filoviruses the influenza peptide had immune suppressive activity ... Knudsen S, Frydenberg J, Clark B, Leffers H. Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms ...
... the ribosome interacts with protein factors such as the elongation factors Tu (EF-Tu) and G (EF-G), that are important players ... After spontaneous peptidyl transfer, the nascent peptide is covalently attached to the A-site tRNA. (ii) The elongation factor ... Peptides containing an L-amino acid and their carrier tRNA is colored in black. Peptides containing a D-amino acid and their ... During elongation, the mRNA-programmed ribosome is presented with an amino acid by a tRNA in complex with elongation factor Tu ...
Peptide Elongation Factor Tu - metabolism , Amino Acids - metabolism , RNA, Transfer, Pro - genetics , RNA, Transfer, Glu - ... Peptide Elongation Factors - metabolism , Protein Biosynthesis , Peptide Chain Elongation, Translational , Saccharomyces ... Peptides , Antibiotics , Analysis , Chemical properties , Structure , Health aspects , Transfer RNA , Proteins , Enzymes , E ... Peptide Elongation Factor Tu - genetics , Glutamate-tRNA Ligase - chemistry , Protein-Serine-Threonine Kinases - metabolism , ...
The aminoacyl tRNA possessing the anticodon to the codon in the A site forms a complex with the elongation factor EF-Tu and GTP ... Which have signal peptides, prokaryotes or eukaryotes? What is the signal peptide hypothesis? ... Eukaryotic protein synthesis initiation has more and different factors. Know that eIF-4E (eukaryotic initiation factor 4E) is ... Translocation: The signal peptide enters the ER lumen; protein elongation continues; the signal peptide is removed by signal ...
EF-Tu: elongation factor thermo unstable. EGF: epidermal growth factor. elf18: 18-residue peptide from EF-TU ... or EF-Tu [10], while DAMPs could be extracellular ATP [11], oligogalacturonides released from pectin [12] or plant peptides ... Direct transcriptional control of the Arabidopsis immune receptor FLS2 by the ethylene-dependent transcription factors EIN3 and ... Elongation factor 1-α (EF1-α) was used as a loading control ... Perception of the bacterial PAMP EF-Tu by the receptor EFR ...
Elongation factor Tu mutants expand amino acid tolerance of protein biosynthesis system.. Yoshio Doi, Takashi Ohtsuki, ... Dissecting limiting factors of the Protein synthesis Using Recombinant Elements (PURE) system.. Li J, Zhang C, Huang P, Kuru E ... Nascent peptide in the ribosome exit tunnel affects functional properties of the A-site of the peptidyl transferase center.. ... Selection of peptides targeting helix 31 of bacterial 16S ribosomal RNA by screening M13 phage-display libraries.. Tek N ...
The former included proteins involved in mRNA translation (i.e. Elongation factor Tu and G, 50 s and 30 s ribosomal proteins), ... Maximum missed cleavages for trypsin was set at 1, peptide charge at 2+ and 3+, peptide tolerance at +/- 1.5 Da, and MS/MS ... Peptides were analyzed by capillary-HPLC-electrospray tandem mass spectrometry (HPLC-ESI-MS/MS) on a Thermo Fisher LTQ ion trap ... Kadioglu A, Weiser JN, Paton JC, Andrew PW: The role of Streptococcus pneumoniae virulence factors in host respiratory ...
... the 60 kDa chaperonin of Pseudomonas fluorescens and elongation factor-Tu of Yersinia pestis. The results strongly suggest that ... Moreover, peptides were selected from the VP2 amino acid sequence and use to raise polyclonal chicken anti-VP2 peptide ... Currently vaccines are used to control IBDV infection, however, their efficacy is affected by factors such as the presence of ... It is believed that the bacterial proteins contain common peptides with chicken proteins of the chicken genome which has not ...
... and the polypeptide chain elongation factor Tu (tufb) promoter, without being limited thereto. ... Peptides and compositions which modulate apoptosis. US6544523 *. 12 Nov 1997. 8 Apr 2003. Chiron Corporation. Mutant forms of ... If desired, the DNA sequence encoding the signal peptide sequence of a yeast gene may be linked to the DNA to be expressed in ... The dose will vary, depending on factors such as the condition, age and body weight of the patient, but usually it may be ...
Till now, it is still unclear how proteins such as GroEL and elongation factor TU, leaving the bacterial cell, are retained on ... The peptides were bound to the ZipTip pipet tip by aspirating and dispensing the sample for at least 15 cycles, washed with 0.1 ... Additionally, there are 49 proteins with predicted signal peptide in the 309 identified cell wall proteins (Fig. 4A).. ... can be considered putative virulence factors as they have previously been suggested to play some role in virulence [38-52]. ...
  • Our analysis demonstrates differential binding affinities of two receptors with a family of peptide ligands and the corresponding physiological effects of the specific receptor-ligand interactions. (plantcell.org)
  • It is believed that the bacterial proteins contain common peptides with chicken proteins of the chicken genome which has not been fully annotated as yet. (ukzn.ac.za)
  • Besides flg22, the mutants respond with a reduced calcium elevation to several other MAMPs and a plant endogenous peptide that is proteolytically processed from pre-pro-proteins during wounding. (biomedcentral.com)
  • Mannose 6-phosphate/insulin-like growth factor-II receptor targets the urokinase receptor to lysosomes via a novel binding interaction. (labome.ru)
  • Moreover, peptides were selected from the VP2 amino acid sequence and use to raise polyclonal chicken anti-VP2 peptide antibodies for comparative identification against chicken anti-VP2 antibodies of possible IBDV receptor(s). (ukzn.ac.za)
  • Regulation of translation elongation controls not only the continuous and ubiquitous expression of immediate early genes, but also the expression of a large number of gene transcripts, which may be arrested in certain rapidly reversible conditions such as starvation [ 8 - 11 ]. (mdpi.com)
  • However, EF-Tu has evolved the capacity to execute diverse functions on the extracellular surface of both eukaryote and prokaryote cells. (frontiersin.org)
  • EF-Tu can traffic to, and is retained on, cell surfaces where can interact with membrane receptors and with extracellular matrix on the surface of plant and animal cells. (frontiersin.org)
  • To effect alternate virulence-associated functions, including adhesion to host extracellular matrix components, EF-Tu must gain access and be retained on the extracellular surface. (frontiersin.org)
  • Thiopeptides, or thiazolyl peptides, are a relatively new family of antibiotics that already counts with more than one hundred different entities. (mdpi.com)
  • Currently vaccines are used to control IBDV infection, however, their efficacy is affected by factors such as the presence of maternally derived antibodies in young chickens which reduces vaccine load, the continuous emergence of new virulent IBDV strains and bursal atrophy caused by some vaccines. (ukzn.ac.za)
  • Diverse functions have been ascribed to EF-Tu many of which include important virulence traits in Gram positive and Gram-negative pathogenic bacteria. (frontiersin.org)