This article needs additional citations for
verification. (October 2019) |
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]
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 ( β γ) [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]
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]
This article needs additional citations for
verification. (October 2019) |
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]
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 ( β γ) [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]
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]