(R)-ß-lysine-modified elongation factor P functions in translation elongation.
J Biol Chem
; 288(6): 4416-23, 2013 Feb 08.
Article
em En
| MEDLINE
| ID: mdl-23277358
ABSTRACT
Post-translational modification of bacterial elongation factor P (EF-P) with (R)-ß-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-(ß)-lysyl-EF-P showed 30% increased puromycin reactivity but no differences in dipeptide synthesis rates when compared with the ß-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 ß-lysylation but not hydroxylation.
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Base de dados:
MEDLINE
Assunto principal:
Elongação Traducional da Cadeia Peptídica
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Proteínas de Bactérias
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Fatores de Alongamento de Peptídeos
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Processamento de Proteína Pós-Traducional
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Salmonella enterica
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Lisina
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article