Two residues predominately dictate functional difference in motility between Shewanella oneidensis flagellins FlaA and FlaB [Protein Synthesis and Degradation]

April 14th, 2014 by Sun, L., Dong, Y., Shi, M., Jin, M., Zhou, Q., Luo, Z.-Q., Gao, H.

Nearly half of flagellated microorganisms possess a multiple-flagellin system. While a functional filament can be formed from one of multiple flagellins alone in many bacteria, it is more common that one flagellin is the major constituent and others contribute. Underlying mechanisms proposed for such scenarios cover flagellin regulation of various levels, including transcription, translation, post-translational modification, secretion, and filament assembly. In Shewanella oneidensis, the flagellar filament is composed of FlaA and FlaB flagellins; the latter is the major one in terms of motility. In this study we showed that regulation of all levels except for filament assembly is indistinguishable between these two flagellins. Further analyses revealed that two amino acid residues predominately dictated functional difference with respect to motility. Given that Shewanella prefer a solid-surface associated life style, to which filaments consisting of either FlaA or FlaB are equally supportive, we envision that roles of flagella in surface adhesion and formation of bacterial communities are particularly important for their survival and proliferation in these specific niches.
  • Posted in Journal of Biological Chemistry, Publications
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