Predicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species.

ABSTRACT:

Background

The bacterial elongation factor P (EF-P) is strictly conserved in bacteria and essential for protein synthesis. It is homologous to the eukaryotic translation initiation factor 5A (eIF5A). A highly conserved eIF5A lysine is modified into an unusual amino acid derived from spermidine, hypusine. Hypusine is absolutely required for eIF5A's role in translation in Saccharomyces cerevisiae. The homologous lysine of EF-P is also modified to a spermidine derivative in Escherichia coli. However, the biosynthesis pathway of this modification in the bacterial EF-P is yet to be elucidated.

Presentation of the hypothesis

Here we propose a potential mechanism for the post-translational modification of EF-P. By using comparative genomic methods based on physical clustering and p

SUBMITTER: Bailly M 

PROVIDER: S-EPMC2821294 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature