Biochemical characterization of the flagellar stator-associated inner membrane protein FliL from Vibrio alginolyticus

被引：7

作者：

Kumar, Ananthanarayanan ^{[1
,5
]}

Isumi, Miyu ^{[2
]}

Sakuma, Mayuko ^{[1
,3
]}

Zhu, Shiwei ^{[1
,6
]}

Nishino, Yuuki ^{[1
]}

Onoue, Yasuhiro ^{[1
]}

Kojima, Seiji ^{[1
]}

Miyanoiri, Yohei ^{[4
]}

Imada, Katsumi ^{[2
]}

Homma, Michio ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Sci, Div Biol Sci, Chikusa Ku, Furo Cho, Nagoya, Aichi 4648602, Japan

[2] Osaka Univ, Grad Sch Sci, Dept Macromol Sci, 1-1 Machikaneyama, Toyonaka, Osaka 5600043, Japan

[3] Nagoya Univ, Radioisotope Res Ctr, Chikusa Ku, Nagoya, Aichi 4648602, Japan

[4] Grad Sch Sci, Struct Biol Res Ctr, Nagoya, Aichi, Japan

[5] MRC Lab Mol Biol, Francis Crick Ave, Cambridge CB2 0QH, England

[6] John P & Kathrine G McGovern Med Sch, Dept Pathol & Lab Med, 6431 Fannin St, Houston, TX 77030 USA

来源：

JOURNAL OF BIOCHEMISTRY | 2017年 / 161卷 / 04期

关键词：

polar flagella; crystal structure; NMR; periplasm; bacteria; MOTOR; GENE; MOTILITY;

D O I：

10.1093/jb/mvw076

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The flagellar motor is embedded in the cell envelope and rotates upon interaction between the stator and the rotor. The rotation is powered by ion flow through the stator. A single transmembrane protein named FliL is associated with torque generation in the flagellar motor. We established an Escherichia coli over-expression system for FliL of Vibrio alginolyticus, a marine bacterium that has a sodium-driven polar flagellum. We successfully expressed, purified, and crystallized the ca. 17 kDa full-length FliL protein and generated a construct that expresses only the ca. 14 kDa periplasmic region of FliL (Delta TM FliL). Biochemical characterization and NMR analysis revealed that Delta TM FliL weakly interacted with itself to form an oligomer. We speculate that the observed dynamic interaction may be involved in the role of FliL in flagellar motor function.

引用

页码：331 / 337

页数：7

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