In situ structure of the Caulobacter crescentus flagellar motor and visualization of binding of a CheY-homolog.
Bacterial Proteins
/ genetics
Caulobacter crescentus
/ metabolism
Electron Microscope Tomography
Flagella
/ metabolism
Genome, Bacterial
Image Processing, Computer-Assisted
Membrane Proteins
/ genetics
Methyl-Accepting Chemotaxis Proteins
/ metabolism
Models, Molecular
Mutation
Protein Binding
Structure-Activity Relationship
Caulobacter crescentus
CheY
cyclic-di-GMP
effector binding
subtomogram averaging
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
11
03
2020
revised:
30
04
2020
accepted:
04
05
2020
pubmed:
26
5
2020
medline:
10
6
2021
entrez:
26
5
2020
Statut:
ppublish
Résumé
Bacterial flagellar motility is controlled by the binding of CheY proteins to the cytoplasmic switch complex of the flagellar motor, resulting in changes in swimming speed or direction. Despite its importance for motor function, structural information about the interaction between effector proteins and the motor are scarce. To address this gap in knowledge, we used electron cryotomography and subtomogram averaging to visualize such interactions inside Caulobacter crescentus cells. In C. crescentus, several CheY homologs regulate motor function for different aspects of the bacterial lifestyle. We used subtomogram averaging to image binding of the CheY family protein CleD to the cytoplasmic Cring switch complex, the control center of the flagellar motor. This unambiguously confirmed the orientation of the motor switch protein FliM and the binding of a member of the CheY protein family to the outside rim of the C ring. We also uncovered previously unknown structural elaborations of the alphaproteobacterial flagellar motor, including two novel periplasmic ring structures, and the stator ring harboring eleven stator units, adding to our growing catalog of bacterial flagellar diversity.
Identifiants
pubmed: 32449846
doi: 10.1111/mmi.14525
pmc: PMC7534056
doi:
Substances chimiques
Bacterial Proteins
0
Membrane Proteins
0
Methyl-Accepting Chemotaxis Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
443-453Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L023091/1
Pays : United Kingdom
Informations de copyright
© 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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