Carbonyl reduction by YmfI in Bacillus subtilis prevents accumulation of an inhibitory EF‐P modification state |
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| Authors: | Katherine R. Hummels Anne Witzky Andrei Rajkovic Rodney Tollerson II Lisa A. Jones Michael Ibba Daniel B. Kearns |
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| Affiliation: | 1. Department of Biology, Indiana University, Bloomington, IN 47405, USA;2. Department of Molecular Genetics and Center for RNA Biology, Ohio State University, Columbus, OH 43210, USA;3. Department of Microbiology and Center for RNA Biology, Ohio State University, Columbus, OH 43210, USA;4. Proteomics Facility, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109 |
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| Abstract: | Translation elongation factor P (EF‐P) in Bacillus subtilis is required for a form of surface migration called swarming motility. Furthermore, B. subtilis EF‐P is post‐translationally modified with a 5‐aminopentanol group but the pathway necessary for the synthesis and ligation of the modification is unknown. Here we determine that the protein YmfI catalyzes the reduction of EF‐P‐5 aminopentanone to EF‐P‐5 aminopentanol. In the absence of YmfI, accumulation of 5‐aminopentanonated EF‐P is inhibitory to swarming motility. Suppressor mutations that enhanced swarming in the absence of YmfI were found at two positions on EF‐P, including one that changed the conserved modification site (Lys 32) and abolished post‐translational modification. Thus, while modification of EF‐P is thought to be essential for EF‐P activity, here we show that in some cases it can be dispensable. YmfI is the first protein identified in the pathway leading to EF‐P modification in B. subtilis, and B. subtilis encodes the first EF‐P ortholog that retains function in the absence of modification. |
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