Elongation factor

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 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]

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]}

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]

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]

• Alberts, 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]}

• nobelprize.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