Arginine-rhamnosylation as new strategy to activate translation elongation factor P
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چکیده
منابع مشابه
Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline-specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved the crystal structure of EarP from Pse...
متن کاملMaintenance of Transcription-Translation Coupling by Elongation Factor P
UNLABELLED Under conditions of tight coupling between translation and transcription, the ribosome enables synthesis of full-length mRNAs by preventing both formation of intrinsic terminator hairpins and loading of the transcription termination factor Rho. While previous studies have focused on transcription factors, we investigated the role of Escherichia coli elongation factor P (EF-P), an elo...
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Translation elongation factor P (EF-P), a ubiquitous protein over the entire range of bacterial species, rescues ribosomal stalling at consecutive prolines in proteins. In Escherichia coli and Salmonella enterica, the post-translational β-lysyl modification of Lys34 of EF-P is important for the EF-P activity. The β-lysyl EF-P modification pathway is conserved among only 26-28% of bacteria. Rece...
متن کامل(R)-β-lysine-modified elongation factor P functions in translation elongation.
Post-translational modification of bacterial elongation factor P (EF-P) with (R)-β-lysine at a conserved lysine residue activates the protein in vivo and increases puromycin reactivity of the ribosome in vitro. The additional hydroxylation of EF-P at the same lysine residue by the YfcM protein has also recently been described. The roles of modified and unmodified EF-P during different steps in ...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2015
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio.1751