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Elongation factor

April 15, 2024

Not to be confused with Relative elongation.
"EF2" and "EF-2" redirect here. For the tornado intensity rating, see Enhanced Fujita scale § Parameters.

Elongation factors are a set of proteins that function at the ribosome, during protein synthesis, to facilitate translational elongation from the formation of the first to the last peptide bond of a growing polypeptide. Most common elongation factors in prokaryotes are EF-Tu, EF-Ts, EF-G.[1] Bacteria and eukaryotes use elongation factors that are largely homologous to each other, but with distinct structures and different research nomenclatures.[2]

Ternary complex of EF-Tu (blue), tRNA (red) and GTP (yellow). Taken from PDB Molecule of the Month Elongation factors, September 2006.

Elongation is the most rapid step in translation.[3] In bacteria, it proceeds at a rate of 15 to 20 amino acids added per second (about 45-60 nucleotides per second).[citation needed] In eukaryotes the rate is about two amino acids per second (about 6 nucleotides read per second).[citation needed] Elongation factors play a role in orchestrating the events of this process, and in ensuring the high accuracy translation at these speeds.[citation needed]

Nomenclature of homologous EFs edit

Elongation factors
Bacterial Eukaryotic/Archaeal Function
EF-Tu eEF-1A (α)[2] mediates the entry of the aminoacyl tRNA into a free site of the ribosome.[4]
EF-Ts eEF-1B (βγ)[2] serves as the guanine nucleotide exchange factor for EF-Tu, catalyzing the release of GDP from EF-Tu.[2]
EF-G eEF-2 catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation. Causes large conformation changes.[5]
EF-P eIF-5A possibly stimulates formation of peptide bonds and resolves stalls.[6]
EF-4 (None) Proofreading
Note that EIF5A, the archaeal and eukaryotic homolog to EF-P, was named as an initiation factor but now considered an elongation factor as well.[6]

In addition to their cytoplasmic machinery, eukaryotic mitochondria and plastids have their own translation machinery, each with their own set of bacterial-type elongation factors.[7][8] In humans, they include TUFM, TSFM, GFM1, GFM2, GUF1; the nominal release factor MTRFR may also play a role in elongation.[9]

In bacteria, selenocysteinyl-tRNA requires a special elongation factor SelB (P14081) related to EF-Tu. A few homologs are also found in archaea, but the functions are unknown.[10]

As a target edit

Elongation factors are targets for the toxins of some pathogens. For instance, Corynebacterium diphtheriae produces diphtheria toxin, which alters protein function in the host by inactivating elongation factor (EF-2). This results in the pathology and symptoms associated with diphtheria. Likewise, Pseudomonas aeruginosa exotoxin A inactivates EF-2.[11]

References edit

  1. ^ Parker, J. (2001). "Elongation Factors; Translation". Encyclopedia of Genetics. pp. 610–611. doi:10.1006/rwgn.2001.0402. ISBN 9780122270802.
  2. ^ a b c d Sasikumar, Arjun N.; Perez, Winder B.; Kinzy, Terri Goss (July 2012). "The Many Roles of the Eukaryotic Elongation Factor 1 Complex". Wiley Interdisciplinary Reviews. RNA. 3 (4): 543–555. doi:10.1002/wrna.1118. ISSN 1757-7004. PMC 3374885. PMID 22555874.
  3. ^ Prabhakar, Arjun; Choi, Junhong; Wang, Jinfan; Petrov, Alexey; Puglisi, Joseph D. (July 2017). "Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination". Protein Science. 26 (7): 1352–1362. doi:10.1002/pro.3190. ISSN 0961-8368. PMC 5477533. PMID 28480640.
  4. ^ Weijland A, Harmark K, Cool RH, Anborgh PH, Parmeggiani A (March 1992). "Elongation factor Tu: a molecular switch in protein biosynthesis". Molecular Microbiology. 6 (6): 683–8. doi:10.1111/j.1365-2958.1992.tb01516.x. PMID 1573997.
  5. ^ Jørgensen, R; Ortiz, PA; Carr-Schmid, A; Nissen, P; Kinzy, TG; Andersen, GR (May 2003). "Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase". Nature Structural Biology. 10 (5): 379–85. doi:10.1038/nsb923. PMID 12692531. S2CID 4795260.
  6. ^ a b Rossi, D; Kuroshu, R; Zanelli, CF; Valentini, SR (2013). "eIF5A and EF-P: two unique translation factors are now traveling the same road". Wiley Interdisciplinary Reviews. RNA. 5 (2): 209–22. doi:10.1002/wrna.1211. PMID 24402910. S2CID 25447826.
  7. ^ Manuell, Andrea L; Quispe, Joel; Mayfield, Stephen P; Petsko, Gregory A (7 August 2007). "Structure of the Chloroplast Ribosome: Novel Domains for Translation Regulation". PLOS Biology. 5 (8): e209. doi:10.1371/journal.pbio.0050209. PMC 1939882. PMID 17683199.
  8. ^ G C Atkinson; S L Baldauf (2011). "Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms". Molecular Biology and Evolution. 28 (3): 1281–92. doi:10.1093/molbev/msq316. PMID 21097998.
  9. ^ "KEGG DISEASE: Combined oxidative phosphorylation deficiency". www.genome.jp.
  10. ^ Atkinson, Gemma C; Hauryliuk, Vasili; Tenson, Tanel (21 January 2011). "An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea". BMC Evolutionary Biology. 11 (1): 22. doi:10.1186/1471-2148-11-22. PMC 3037878. PMID 21255425.
  11. ^ Lee H, Iglewski WJ (1984). "Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A". Proc. Natl. Acad. Sci. U.S.A. 81 (9): 2703–7. Bibcode:1984PNAS...81.2703L. doi:10.1073/pnas.81.9.2703. PMC 345138. PMID 6326138.

Further reading edit

External links edit

April 15, 2024
elongation, factor, confused, with, relative, elongation, redirect, here, tornado, intensity, rating, enhanced, fujita, scale, parameters, this, article, needs, additional, citations, verification, please, help, improve, this, article, adding, citations, relia. Not to be confused with Relative elongation EF2 and EF 2 redirect here For the tornado intensity rating see Enhanced Fujita scale Parameters This article needs additional citations for verification Please help improve this article by adding citations to reliable sources Unsourced material may be challenged and removed Find sources Elongation factor news newspapers books scholar JSTOR October 2019 Learn how and when to remove this template message Elongation factors are a set of proteins that function at the ribosome during protein synthesis to facilitate translational elongation from the formation of the first to the last peptide bond of a growing polypeptide Most common elongation factors in prokaryotes are EF Tu EF Ts EF G 1 Bacteria and eukaryotes use elongation factors that are largely homologous to each other but with distinct structures and different research nomenclatures 2 Ternary complex of EF Tu blue tRNA red and GTP yellow Taken from PDB Molecule of the Month Elongation factors September 2006 Elongation is the most rapid step in translation 3 In bacteria it proceeds at a rate of 15 to 20 amino acids added per second about 45 60 nucleotides per second citation needed In eukaryotes the rate is about two amino acids per second about 6 nucleotides read per second citation needed Elongation factors play a role in orchestrating the events of this process and in ensuring the high accuracy translation at these speeds citation needed Contents 1 Nomenclature of homologous EFs 2 As a target 3 References 4 Further reading 5 External linksNomenclature of homologous EFs editElongation factors Bacterial Eukaryotic Archaeal FunctionEF Tu eEF 1A a 2 mediates the entry of the aminoacyl tRNA into a free site of the ribosome 4 EF Ts eEF 1B bg 2 serves as the guanine nucleotide exchange factor for EF Tu catalyzing the release of GDP from EF Tu 2 EF G eEF 2 catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation Causes large conformation changes 5 EF P eIF 5A possibly stimulates formation of peptide bonds and resolves stalls 6 EF 4 None ProofreadingNote that EIF5A the archaeal and eukaryotic homolog to EF P was named as an initiation factor but now considered an elongation factor as well 6 In addition to their cytoplasmic machinery eukaryotic mitochondria and plastids have their own translation machinery each with their own set of bacterial type elongation factors 7 8 In humans they include TUFM TSFM GFM1 GFM2 GUF1 the nominal release factor MTRFR may also play a role in elongation 9 In bacteria selenocysteinyl tRNA requires a special elongation factor SelB P14081 related to EF Tu A few homologs are also found in archaea but the functions are unknown 10 As a target editElongation factors are targets for the toxins of some pathogens For instance Corynebacterium diphtheriae produces diphtheria toxin which alters protein function in the host by inactivating elongation factor EF 2 This results in the pathology and symptoms associated with diphtheria Likewise Pseudomonas aeruginosa exotoxin A inactivates EF 2 11 References edit Parker J 2001 Elongation Factors Translation Encyclopedia of Genetics pp 610 611 doi 10 1006 rwgn 2001 0402 ISBN 9780122270802 a b c d Sasikumar Arjun N Perez Winder B Kinzy Terri Goss July 2012 The Many Roles of the Eukaryotic Elongation Factor 1 Complex Wiley Interdisciplinary Reviews RNA 3 4 543 555 doi 10 1002 wrna 1118 ISSN 1757 7004 PMC 3374885 PMID 22555874 Prabhakar Arjun Choi Junhong Wang Jinfan Petrov Alexey Puglisi Joseph D July 2017 Dynamic basis of fidelity and speed in translation Coordinated multistep mechanisms of elongation and termination Protein Science 26 7 1352 1362 doi 10 1002 pro 3190 ISSN 0961 8368 PMC 5477533 PMID 28480640 Weijland A Harmark K Cool RH Anborgh PH Parmeggiani A March 1992 Elongation factor Tu a molecular switch in protein biosynthesis Molecular Microbiology 6 6 683 8 doi 10 1111 j 1365 2958 1992 tb01516 x PMID 1573997 Jorgensen R Ortiz PA Carr Schmid A Nissen P Kinzy TG Andersen GR May 2003 Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase Nature Structural Biology 10 5 379 85 doi 10 1038 nsb923 PMID 12692531 S2CID 4795260 a b Rossi D Kuroshu R Zanelli CF Valentini SR 2013 eIF5A and EF P two unique translation factors are now traveling the same road Wiley Interdisciplinary Reviews RNA 5 2 209 22 doi 10 1002 wrna 1211 PMID 24402910 S2CID 25447826 Manuell Andrea L Quispe Joel Mayfield Stephen P Petsko Gregory A 7 August 2007 Structure of the Chloroplast Ribosome Novel Domains for Translation Regulation PLOS Biology 5 8 e209 doi 10 1371 journal pbio 0050209 PMC 1939882 PMID 17683199 G C Atkinson S L Baldauf 2011 Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms Molecular Biology and Evolution 28 3 1281 92 doi 10 1093 molbev msq316 PMID 21097998 KEGG DISEASE Combined oxidative phosphorylation deficiency www genome jp Atkinson Gemma C Hauryliuk Vasili Tenson Tanel 21 January 2011 An ancient family of SelB elongation factor like proteins with a broad but disjunct distribution across archaea BMC Evolutionary Biology 11 1 22 doi 10 1186 1471 2148 11 22 PMC 3037878 PMID 21255425 Lee H Iglewski WJ 1984 Cellular ADP ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A Proc Natl Acad Sci U S A 81 9 2703 7 Bibcode 1984PNAS 81 2703L doi 10 1073 pnas 81 9 2703 PMC 345138 PMID 6326138 Further reading editAlberts B et al 2002 Molecular Biology of the Cell 4th ed New York Garland Science ISBN 0 8153 3218 1 page needed Berg J M et al 2002 Biochemistry 5th ed New York W H Freeman and Company ISBN 0 7167 3051 0 page needed Singh B D 2002 Fundamentals of Genetics New Delhi India Kalyani Publishers ISBN 81 7663 109 4 page needed External links editnobelprize org Explaining the function of eukaryotic elongation factors Elongation Factor at the U S National Library of Medicine Medical Subject Headings MeSH Peptide Elongation Factor G at the U S National Library of Medicine Medical Subject Headings MeSH Peptide Elongation Factor Tu at the U S National Library of Medicine Medical Subject Headings MeSH EC 3 6 5 3 Retrieved from https en wikipedia org w index php title Elongation factor amp oldid 1185006700, wikipedia, wiki, book, books, library,

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