Deletion analysis of the carboxyl-terminal region of the PomB component of the vibrio alginolyticus polar flagellar motor.
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 DeltapomB 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.
Yakushi
Toshiharu
T
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya 464-8602, Japan. 4juji@cc.nagoya-u.ac.jp
Hattori
Naoko
N
Homma
Michio
M
D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology; D005407:Flagella / Q000235:genetics* / Q000502:physiology; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology; D009068:Movement / Q000502:physiology; D011485:Protein Binding; D017384:Sequence Deletion; D015222:Sodium Channels / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D044149:Vibrio alginolyticus / Q000235:genetics*
D001426:Bacterial Proteins; D008565:Membrane Proteins; C107540:PomA protein, Vibrio; C107541:PomB protein, Vibrio; D015222:Sodium Channels