FliL ring enhances the function of periplasmic flagella

Author:

Guo Shuaiqi12,Xu Hui3,Chang Yunjie12,Motaleb Md A.3ORCID,Liu Jun12ORCID

Affiliation:

1. Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536

2. Microbial Sciences Institute, Yale University, West Haven, CT 06516

3. Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC 27834

Abstract

Significance How flagella sense complex environments and control bacterial motility remain fascinating questions. Here, we deploy cryo-electron tomography to determine in situ structures of the flagellar motor in wild-type and mutant cells of Borrelia burgdorferi , revealing that three flagellar proteins (FliL, MotA, and MotB) form a unique supramolecular complex in situ. Importantly, FliL not only enhances motor function by forming a ring around the stator complex MotA/MotB in its extended, active conformation but also facilitates assembly of the stator complex around the motor. Our in situ data provide insights into how cooperative remodeling of the FliL–stator supramolecular complex helps regulate the collective ion flux and establishes the optimal function of the flagellar motor to guide bacterial motility in various environments.

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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