TY - JOUR. T1 - Biosynthetic incorporation of [3H]ethanolamine into protein synthesis elongation factor 1α reveals a new post-translational protein modification. AU - Rosenberry, T. L.. AU - Krall, J. A.. AU - Dever, T. E.. AU - Haas, R.. AU - Louvard, D.. AU - Merrick, W. C.. PY - 1989/1/1. Y1 - 1989/1/1. N2 - Biosynthetic incorporation of [3H]ethanolamine into proteins was assessed in the human erythroleukemia cell line K562. A single predominant labeled protein of about 50 kDa was observed following electrophoresis of cell extracts on polyacrylamide gels in the presence of sodium dodecyl sulfate. Subcellular fractionation showed this protein to distribute similarly to a 46-kDa [3H]ethanolamine-labeled protein reported previously (Tisdale, E.J., and Tartakoff, A.M. (1988) J. Biol. Chem. 263, 8244-8252). In particular, the protein was enriched in cytosolic and microsomal fractions relative to plasma membrane and thus did not appear to correspond to the class of proteins with glycoinositol ...
canSAR Domains and Structures of B7KGU8 | efp | Elongation factor P - Also known as EFP_GLOC7, efp. Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Based on previous work,23,24 we chose a strategy for glycopeptide synthesis that involves direct silver-promoted glycosylation between an S-alkyl-isothiourea and the amine of the amino acid side chain on the solid phase. First, we synthesized the key building block, N-glycosyl-S-alkyl-isothiourea 6, starting from L-rhamnose 2 (Fig. 3b): glycosyl chloride 3 in the desired configuration was obtained using well established procedures (85% yield).25,26 Subsequently, 3 was treated with potassium thiocyanate (KSCN) and tetrabutylammonium hydrogen iodide (TBAI) in anhydrous acetonitrile to get glycosyl isothiocyanate 4 (70% yield).27 Next, glycosyl thiourea 5 was prepared via ammoniation of 4 in tetrahydrofuran (99% yield).28 Finally, a two-step, one-pot procedure converted 5 into 6 in the presence of ethyl iodide and tert-butoxycarbonyl anhydride (75% yield).29 Taken together from 2 to 6 we ended up with an efficiency of about 44%. The configuration of the attached rhamnose in the hapten depends on ...
At crucial points in the metabolism of all organisms, a protein with the unwieldy name of Translation Elongation Factor P (EF-P, for short) takes center stage. What it actually does during protein synthesis has only now been elucidated - by researchers at LMU.. The research group led by Kirsten Jung, Professor of Microbiology at LMU, actually focused on how bacteria cope with stress, for example how the receptor meolecule CadC monitors the acidity in the environment and alerts the cell to take countermeasures to protect itself. However, one day Kirsten Jung found herself asking questions about protein synthesis, the core biosynthetic process that makes all metabolism possible. This arose because she discovered that, in the absence of Elongation Factor P, the cell doesn´t make enough CadC to carry out its job effectively.. Recovering from a stall. How then does EF-P regulate protein synthesis in general, and, in particular, the synthesis of CadC? In collaboration with Daniel Wilson´s group at ...
Ribosomal protein P2 alpha, a component of the ribosomal stalk, which is involved in the interaction between translational elongation factors and the ...
Ribosomal protein P2 beta, a component of the ribosomal stalk, which is involved in the interaction between translational elongation factors and the ...
The highly conserved Nus factors of bacteria were discovered as essential host proteins for the growth of temperate phage λ in Escherichia coli. Later, their essentiality and functions in transcription, translation, and, more recently, in DNA repair have been elucidated. Close involvement of these factors in various gene networks and circuits is also emerging from recent genomic studies. We have described a detailed overview of their biochemistry, structures, and various cellular functions, as well as their interactions with other macromolecules. Towards the end, we have envisaged different uncharted areas of studies with these factors, including their participation in pathogenicity.
Molecular model of elongation factor complexed with GDP (guanosine diphosphate). This enzyme is involved in the elongation of polypeptide chains during translation, the production of a protein from an mRNA (messenger ribonucleic acid) template. - Stock Image C025/1936
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. 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.
Ribosomal elongation factor 4 (EF4) is highly conserved among bacteria, mitochondria, and chloroplasts. However, the EF4-encoding gene, lepA, is nonessential an
Buy our Recombinant |em|E. coli |/em| nusA protein. Ab78932 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam…
An epitope of elongation factor Tu (EF-Tu), which is found in organisms in both the bacterial and archaeal domains, was recently defined by mAb 900. To localize the conserved epitope within the EF-Tu molecule and to determine its sequence, SPOTScan analysis of synthetic peptides, Western blot analysis of purified EF-Tu domains and site-directed mutagenesis studies were used. Analysis of mAb 900 binding to overlapping 15-mer peptides encompassing the complete sequence of EF-Tu of Escherichia coli was inconclusive, suggesting three distinct regions may be epitopes. Western blot analysis of EF-Tu domains 1-3 of Thermus thermophilus suggested that the epitope was located at the N terminus. This was confirmed by site-directed mutagenesis of EF-Tu domain 1 of Mycoplasma hominis. By C-terminal truncation of the N-terminal 15-mer peptide the epitope was mapped to EF-Tu residues 1-6. Replacement of each of the residues in the epitope peptide demonstrated that only positions 5 and 6 were indispensable for
Electron paramagnetic resonance spectroscopy has been used to obtain information on the structure and stability of the products of GTP cleavage at the active site of elongation factor Tu (EF-Tu) from Bacillus stearothermophilus. Using stereospecifically labelled (Sp)-(Rp)-[beta-17O]GTP (prepared by modification of a previously published procedure which is now also suitable for guanine nucleotides), it was found that only one of the two possible diastereomers (Sp) led to detectable line-broadening of the EPR spectrum of Mn2+ at the active site of EF-Tu (linewidth 1.5 mT), whereas the Rp isomer caused the same linewidth as unlabelled nucleotide (1.3 mT). From our earlier work and from a demonstration that the lifetime of the state giving the broadened spectrum is too long to be assigned to the EF-Tu.GDP.Mn complex [the rate constant for decay as measured by displacement of GDP by the fluorescent 2(3)-O-(N-methylanthraniloyl)-GDP is 6.2 x 10(-3) s-1 at 25 degrees C and pH 6.8], we conclude that ...
5 million rubles a year for three years will be allocated to this project titled Structural and functional genetic analysis of the elongation factor P and the initiation complex of Staphylococcus aureus. The Structural Biology Lab was established in 2014. This particular project is handled by six KFU employees and two colleagues from other institutions - one from the Institute of Protein Research (Pushschino, Russia) and one from University of Strasbourg. As Dr. Usachev explained, the project concentrates on studying the 3D structure of elongation factor P present in S. aureus. The factor helps ribosomes in synthesizing proteins with polyproline sections which are often the primary causes of virulence. Stopping such mechanism in cells can help eliminate them without affecting human cells. 3D visualization is the first step in creating potent antibiotics for this task. «Different organisms have variations in 3D structure of protein-producing cell mechanisms. Our basic idea is to find the ...
HEADER RNA BINDING PROTEIN 22-NOV-99 1DG1 TITLE WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU). COMPND MOL_ID: 1; COMPND 2 MOLECULE: ELONGATION FACTOR TU; COMPND 3 CHAIN: G, H; COMPND 4 SYNONYM: EF-TU SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 OTHER_DETAILS: CELL CYTOPLASM EXTRACT KEYWDS ELONGATION FACTOR, TRNA BINDING, ALPHA BETA SHIFT, TS KEYWDS 2 BINDING PROTEIN, GTPASE, GDP BINDING, RNA BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.ABEL,M.YODER,R.HILGENFELD,F.JURNAK REVDAT 4 24-FEB-09 1DG1 1 VERSN REVDAT 3 01-APR-03 1DG1 1 JRNL REVDAT 2 29-MAR-00 1DG1 1 REMARK REVDAT 1 01-DEC-99 1DG1 0 JRNL AUTH K.ABEL,M.D.YODER,R.HILGENFELD,F.JURNAK JRNL TITL AN ALPHA TO BETA CONFORMATIONAL SWITCH IN EF-TU. JRNL REF STRUCTURE V. 4 1153 1996 JRNL REFN ISSN 0969-2126 JRNL PMID 8939740 JRNL DOI 10.1016/S0969-2126(96)00123-2 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 ...
tuf2; recname: full=elongation factor tu 2; short=ef-tu 2; recname: full=elongation factor tu 2; short=ef-tu 2; K02358 elongation factor ...
Plant elongation factor EF-1 consists of four subunits (EF-1 alpha beta beta gamma ). EF-1 alpha . GTP catalyses the binding of aminoacyl-tRNA to the ...
ekf:KO11_06105 K02358 elongation factor Tu , (GenBank) tufA; elongation factor Tu (A) MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG ...
ELOF1 - ELOF1 (untagged)-Human elongation factor 1 homolog (S. cerevisiae) (ELOF1) available for purchase from OriGene - Your Gene Company.
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1NZ9: Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus
BLASTX 2.0a19MP-WashU [05-Feb-1998] [Build sol2.5-ultra 01:47:30 05-Feb-1998] Reference: Gish, Warren (1994-1997). unpublished. Gish, Warren and David J. States (1993). Identification of protein coding regions by database similarity search. Nat. Genet. 3:266-72. Notice: statistical significance is estimated under the assumption that the equivalent of one entire reading frame in the query sequence codes for protein and that significant alignments will involve only coding reading frames. Query= CcruzaQ_941 (635 letters) Translating both strands of query sequence in all 6 reading frames Database: /usr/local/db/others/blast/nrdb 322,836 sequences; 97,797,364 total letters. Searching....10....20....30....40....50....60....70....80....90....100% done Smallest Sum Reading High Probability Sequences producing High-scoring Segment Pairs: Frame Score P(N) N A gnl,PID,d1010075 (D50806) elongation factor 2 [Try... +1 1019 4.0e-102 1 A gnl,PID,d1005333 (D21259) elongation factor 2 [Ent... +1 682 2.1e-66 1 A ...
Genetic information processingTranscriptionTranscription factorstranscription termination/antitermination factor NusG (TIGR00922; HMM-score: 203.6) ...
Girodat, D.; Mercier, E.; Gzyl, K. E.; Wieden, H. J.: Elongation factor Tus nucleotide binding is governed by a thermodynamic landscape unique among bacterial translation factors. Journal of the American Chemical Society 141 (26), S. 10236 - 10246 (2019 ...
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Bacterial protein synthesis is intricately connected to metabolic rate. One of the ways in which bacteria respond to environmental stress is through posttranslational modifications of translation factors. Translation elongation factor Tu (EF-Tu) is methylated and phosphorylated in response to nutrient starvation upon entering stationary phase, and its phosphorylation is a crucial step in the pathway toward sporulation. We analyze how phosphorylation leads to inactivation of EF-Tu. We provide structural and biophysical evidence that phosphorylation of EF-Tu at T382 acts as an efficient switch that turns off protein synthesis by decoupling nucleotide binding from the EF-Tu conformational cycle. Direct modifications of the EF-Tu switch I region or modifications in other regions stabilizing the β-hairpin state of switch I result in an effective allosteric trap that restricts the normal dynamics of EF-Tu and enables the evasion of the control exerted by nucleotides on G proteins. These results ...
This gene encodes a multifunctional protein that localizes to both the cytoplasm and nucleus. In the cytoplasm, the encoded protein is an auxiliary component of the macromolecular aminoacyl-tRNA synthase complex. However, its mouse homolog has been shown to translocate to the nucleus in response to DNA damage, and it plays a positive role in ATM/ATR-mediated p53 activation. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream MUTED (muted homolog) gene. An EEF1E1-related pseudogene has been identified on chromosome 2.
Elongation factor thermal unstable Tu (EF-Tu) is a G protein that catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome inside living cells. Structural and biochemical studies have described the complex interactions needed to effect canonical function. However, EF-Tu has evolved the capacity to execute diverse functions on the extracellular surface of both eukaryote and prokaryote cells. 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. Our structural studies indicate that short linear motifs (SLiMs) in surface exposed, non-conserved regions of the molecule may play a key role in the moonlighting functions ascribed to this ancient, highly abundant protein. Here we explore the diverse moonlighting functions relating to pathogenesis of EF-Tu in bacteria and examine putative SLiMs on surface-exposed regions of the molecule.
Like the other amino acids used by cells, selenocysteine has a specialized tRNA. The primary and secondary structure of selenocysteine tRNA, tRNA(Sec), differ from those of standard tRNAs in several respects, most notably in having an 8-base (bacteria) or 9-base (eukaryotes) pair acceptor stem, a long variable region arm, and substitutions at several well-conserved base positions. The selenocysteine tRNAs are initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tRNA(Sec) is not used for translation because it is not recognised by the normal translation factor (EF-Tu in bacteria, EF1alpha in eukaryotes). Rather, the tRNA-bound seryl residue is converted to a selenocysteyl-residue by the pyridoxal phosphate-containing enzyme selenocysteine synthase. Finally, the resulting Sec-tRNA(Sec) is specifically bound to an alternative translational elongation factor (SelB or mSelB) which delivers it in a targeted manner to the ribosomes translating mRNAs for selenoproteins. The ...
This gene encodes a member of the transcription elongation factor A (SII)-like (TCEAL) gene family. This family is comprised of nuclear phosphoproteins that modulate transcription in a promoter context-dependent manner. Multiple family members are located on the X chromosome. Alternatively splicing results in multiple transcript variants. There is a pseudogene for this gene on chromosome 13. [provided by RefSeq, Apr 2015 ...
Complete information for EEF1A1P9 gene (Pseudogene), Eukaryotic Translation Elongation Factor 1 Alpha 1 Pseudogene 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for EEF1A1P10 gene (Pseudogene), Eukaryotic Translation Elongation Factor 1 Alpha 1 Pseudogene 10, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Synthesis of proteins is performed by the ribosome, a large ribonucleoprotein complex. Apart from the ribosome, numerous protein factors participate in this process. Elongation factor 2 (eEF2) is one of these factors. eEF2 is an essential protein with a mol. mass of about 100 kDa. The amino acid sequence of eEF2 is highly conserved in different organisms. eEF2 from S. cerevisiae contains 842 amino acids. The role of eEF2 in protein synthesis is to participate in the translocation of tRNAs from the A- and P-sites on the ribosome to the P- and E-sites. This movement of tRNAs is accompanied by a simultaneous movement of mRNA by one codon. eEF2 consists of six domains referred to as domains G, G′ and II-V, belongs to the G-protein super-family and possesses all structural motifs characterizing proteins in this family. eEF2 binds to the ribosome in complex with GTP. After GTP hydrolysis and translocation, it leaves the ribosome bound to GDP. The rate of protein synthesis in the cell can be ...
Addresses: Bilgin N, Univ Uppsala, Ctr Biomed, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Uppsala Univ, Ctr Biomed, Dept Biol Mol, S-75124 Uppsala, Sweden. Inst Biol Struct, F-38027 Grenoble 1, France. DESY, European Mol Biol Lab, D-22603 Hamburg, GeAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14 ...
Tumor Necrosis Apoptosis Inducing Ligand (TRAIL) is a death ligand with some specificity for transformed cells. However, some cancer cells develop resistance to TRAIL allowing escape from immune surveillance. Re-sensitization of these cells to TRAIL depends on identifying the mechanism of resistance and applying a targeted corrective. We studied several possible mechanisms of TRAIL resistance beginning with FLICE-Like Inhibitory Protein (FLIP). The short isoform of FLIP (FLIPshort) is an effective inhibitor of caspase 8 activation and therefore overexpression of FLIPshort may be a mechanism of TRAIL resistance. We found that downregulation of FLIP short was sufficient to re-sensitize some prostate carcinoma cells to TRAIL. Another mechanism we investigated is mediated by Elongation Factor 2 (EF2) which acilitates ribosomal translocation along mRNA strands. EF2 can be inactivated by phosphorylation or by ADP-ribosylation, thereby inhibiting protein synthesis. During inhibition of protein ...
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome ...
Protein required, along with Dph2p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph2p and ...
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Which factors shape macrozoobenthic communities in tufa springs Results from Austrian meteogene travertine-depositing sites. . 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.
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Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene. This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation. It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa). The inactivation of EF-2 by toxins inhibits protein production in the host, causing symptoms due to loss of function in affected cells. GRCh38: Ensembl release 89: ENSG00000167658 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000034994 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (Mar 1990). "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa ...
The release of paused RNA polymerase II into productive elongation is highly regulated, especially at genes that affect human development and disease. To exert control over this rate-limiting step, we designed sequence-specific synthetic transcription elongation factors (Syn-TEFs). These molecules a …
Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [PUBMED:11297922, PUBMED:11290319]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to ...
A few times recently, Ive been blasting and retrieving sequences from NCBI RefSeq, making phylogenetic trees, and then being shocked to find the odd sequence from Xenopus (frog), Ixodes (tick) or Nematostella (Sea Anemone) sequences nested deeply within the bacterial part of the tree. Also with branches comparable to the length of bacterial branches. Inititally, when I got these sequences, I was very excited. I probably exclaimed something like "Bloody hell! Ticks have another mitochondrial elongation factor EF-Tu and it looks like very recent horizontal gene transfer from beta-proteobacteria!", cos thats what it looks like- the nesting suggesting HGT and the lack of this version in close tick relatives suggesting its recent. Of course such a find would be astounding: HGT into a vertebrate, wow. But then I checked Entrez gene and blasted several upstream and downstream genes. They ALL hit bacterial sequences before eukaryotic ones. The whole scaffold was bacterial. Ive found the same in ...
Nolan, R D.; Grasmuk, H; Hogenauer, G; and Drews, J, "Elongation factor 1 from krebs ii mouse ascites cells. Interaction with guanosine nucleotides and aminoacyl-trna." (1974). Subject Strain Bibliography 1974. 1110 ...
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
ef-tu; highly similar to elongation factor Tu from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 700721 - MGH 78578 (sp,A6TEX7); K02358 elongation factor ...
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (599 aa ...
EF-Tu, shown here from PDB entry 1ttt, performs the important job of shepherding each transfer RNA to the ribosome, powered by a molecule of GTP. EF-Tu is the most plentiful protein in bacterial cells-typically there will be enough that every tRNA may be matched with one. It binds to a tRNA after the proper amino acid has been attached to it. Then, the complex docks into the active site of the ribosome. When the tRNA anticodon matches up correctly the mRNA codon, a signal from the ribosome causes EF-Tu to change shape and the molecule of GTP is cleaved. This causes EF-Tu to let go of the tRNA and leave, allowing the tRNA to enter into the reaction ...
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