期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 6, 页码 4416-4423出版社
ELSEVIER
DOI: 10.1074/jbc.M112.438879
关键词
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资金
- National Institutes of Health [GM 65183]
- Vanier Canada Graduate Scholarships
- Canada Institutes for Health Research [MOP-86683, MSH-87729]
- Natural Sciences and Engineering Research Council of Canada [RGPIN 386286-10]
- Canadian Institutes for Health Research
- Genome Canada
- Canadian Foundation for Innovation
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Wellcome Trust
- AbbVie
- Eli Lilly Canada
- GlaxoSmithKline
- Novartis
- Pfizer
- Takeda
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1040302] Funding Source: National Science Foundation
Post-translational modification of bacterial elongation factor P (EF-P) with (R)-beta-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 translation, and how this correlates to its physiological role in the cell, have recently been linked to the synthesis of polyproline stretches in proteins. Polysome analysis indicated that EF-P functions in translation elongation, rather than initiation as proposed previously. This was further supported by the inability of EF-P to enhance the rate of formation of fMet-Lys or fMet-Phe, indicating that the role of EF-P is not to specifically stimulate formation of the first peptide bond. Investigation of hydroxyl-(beta)-lysyl-EF-P showed 30% increased puromycin reactivity but no differences in dipeptide synthesis rates when compared with the beta-lysylated form. Unlike disruption of the other genes required for EF-P modification, deletion of yfcM had no phenotypic consequences in Salmonella. Taken together, our findings indicate that EF-P functions in translation elongation, a role critically dependent on post-translational beta-lysylation but not hydroxylation.
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