RT Journal Article
SR Electronic
T1 Giant flagellins form thick flagellar filaments in two species of marine Gammaproteobacteria
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 221366
DO 10.1101/221366
A1 Nicholas M. Thomson
A1 Josie L. Ferreira
A1 Teige R. Matthews-Palmer
A1 Morgan Beeby
A1 Mark J. Pallen
YR 2017
UL http://biorxiv.org/content/early/2017/11/17/221366.abstract
AB Flagella, the primary means of motility in bacteria, contain thousands of copies of the protein flagellin in self-assembled helical filaments that function as microscopic propellers. Evolution has presented a wide range of different sizes of flagellin, but the upper reaches of the size distribution have barely been explored. We show here that two species of marine Gammaproteobacteria, Bermanella marisrubri Red65 and Oleivorans marinus 2O1, are motile due to the production of thick, monopolar flagellar filaments. In each case, a ‘giant’ flagellin of more than 1,000 amino acids is the only predicted flagellin protein. Two species of Methylobacterium from the leaves of Arabidopsis thaliana also both possess genes for giant flagellins. However, their flagellar filaments are of similar thickness to bacteria with flagellins half the size. This may be explained by the presence of multiple, smaller, flagellin genes in the Methylobacterium species. This work further illustrates how “the” bacterial flagellum is not a single, ideal structure, but a continuum of evolved machines adapted to a wide range of niches.