Previous Article | Next Article ![]()
Journal of Bacteriology, January 2005, p. 778-784, Vol. 187, No. 2
0021-9193/05/$08.00+0 doi:10.1128/JB.187.2.778-784.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya, Japan
Received 13 July 2004/ Accepted 11 October 2004
The stator of the sodium-driven flagellar motor of Vibrio alginolyticus is a membrane protein complex composed of four PomA and two PomB subunits. PomB has a peptidoglycan-binding motif in the C-terminal region. In this study, four kinds of PomB deletions in the C terminus were constructed. None of the deletion proteins restored motility of the
pomB strain. The PomA protein was coisolated with all of the PomB derivatives under detergent-solubilized conditions. Homotypic disulfide cross-linking of all of the deletion derivatives through naturally occurring Cys residues was detected. We conclude that the C-terminal region of PomB is essential for motor function but not for oligomerization of PomB with itself or PomA.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»