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The Vibrio motor proteins, MotX and MotY, are associated with the basal body of Na + ‐driven flagella and required for stator formation
Author(s) -
Terashima Hiroyuki,
Fukuoka Hajime,
Yakushi Toshiharu,
Kojima Seiji,
Homma Michio
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05435.x
Subject(s) - flagellum , basal body , vibrio alginolyticus , biology , vibrio , ring (chemistry) , basal (medicine) , biophysics , anatomy , biochemistry , bacteria , genetics , chemistry , endocrinology , organic chemistry , insulin , gene
Summary The four motor proteins PomA, PomB, MotX and MotY, which are believed to be stator proteins, are essential for motility by the Na + ‐driven flagella of Vibrio alginolyticus . When we purified the flagellar basal bodies, MotX and MotY were detected in the basal body, which is the supramolecular complex comprised of the rotor and the bushing, but PomA and PomB were not. By antibody labelling, MotX and MotY were detected around the LP ring. These results indicate that MotX and MotY associate with the basal body. The basal body had a new ring structure beneath the LP ring, which was named the T ring. This structure was changed or lost in the basal body from a Δ motX or Δ motY strain. The T ring probably comprises MotX and MotY. In the absence of MotX or MotY, we demonstrated that PomA and PomB were not localized to a cell pole. From the above results, we suggest that MotX and MotY of the T ring are involved in the incorporation and/or stabilization of the PomA/PomB complex in the motor.