Document Type
Article
Publication Date
5-20-2016
Abstract
Elongation factor P (EF-P) accelerates diprolyl synthesis and requires a posttranslational modification to maintain proteostasis. Two phylogenetically distinct EF-P modification pathways have been described and are encoded in the majority of Gram-negative bacteria, but neither is present in Gram-positive bacteria. Prior work suggested that the EF-P-encoding gene (efp) primarily supports Bacillus subtilis swarming differentiation, whereas EF-P in Gram-negative bacteria has a more global housekeeping role, prompting our investigation to determine whether EF-P is modified and how it impacts gene expression in motile cells. We identified a 5-aminopentanol moiety attached to Lys32 of B. subtilis EF-P that is required for swarming motility. A fluorescent in vivo B. subtilis reporter system identified peptide motifs whose efficient synthesis was most dependent on 5-aminopentanol EF-P. Examination of the B. subtilis genome sequence showed that these EF-P-dependent peptide motifs were represented in flagellar genes. Taken together, these data show that, in B. subtilis, a previously uncharacterized posttranslational modification of EF-P can modulate the synthesis of specific diprolyl motifs present in proteins required for swarming motility.
Recommended Citation
Rajkovic, A., Hummels, K.R., Witzky, A., Erickson, S., Gafken, P.R., Whitelegge, J.P., Faull, K.F., Kearns, D.B. and Ibba M. (2016) Translation control of swarming proficiency in Bacillus subtilis by 5-amino-pentanolylated elongation factor P. J. Biol. Chem. 291, 10976-10985. https://doi.org/10.1074/jbc.M115.712091
Copyright
American Society for Biochemistry and Molecular Biology
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
This article was originally published in Journal of Biological Chemistry, volume 291, in 2016. https://doi.org/10.1074/jbc.M115.712091