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Leader peptidase A : ウィキペディア英語版 | Leader peptidase A Leader peptidase A (LepA) is an elongation factor that is thought to back-translocate on the ribosome during the translation of RNA to proteins in all prokaryotes and eukaryotes that have maintained functioning mitochondria. There are three primary elongation factors (EF-G, EF-Tu, EF-Ts) that are known to be the main contributors to facilitate elongation during protein synthesis; due to LepA's now acknowledged proofreading function in translation, scientists are now lobbying to have LepA renamed as EF-4 (elongation factor 4). == Evolutionary background == LepA has a highly conserved sequence. LepA orthologs have been found in bacteria and almost all eukaryotes. The conservation in LepA has been shown to cover the entire protein. More specifically, the amino acid identity of LepA among bacterial orthologs ranges from 55%-68%. Two forms of LepA have been observed; one form of LepA branches with mitochondrial LepA sequences, while the second form branches with cyanobacterial orthologs. These findings demonstrate that LepA is significant for bacteria, mitochondria, and plastids. LepA is absent from archaea.
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