Mechanical stress compromises multicomponent efflux complexes in bacteria.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
17 12 2019
Historique:
pubmed: 28 11 2019
medline: 14 4 2020
entrez: 28 11 2019
Statut: ppublish

Résumé

Physical forces have a profound effect on growth, morphology, locomotion, and survival of organisms. At the level of individual cells, the role of mechanical forces is well recognized in eukaryotic physiology, but much less is known about prokaryotic organisms. Recent findings suggest an effect of physical forces on bacterial shape, cell division, motility, virulence, and biofilm initiation, but it remains unclear how mechanical forces applied to a bacterium are translated at the molecular level. In Gram-negative bacteria, multicomponent protein complexes can form rigid links across the cell envelope and are therefore subject to physical forces experienced by the cell. Here we manipulate tensile and shear mechanical stress in the bacterial cell envelope and use single-molecule tracking to show that octahedral shear (but not hydrostatic) stress within the cell envelope promotes disassembly of the tripartite efflux complex CusCBA, a system used by

Identifiants

pubmed: 31772020
pii: 1909562116
doi: 10.1073/pnas.1909562116
pmc: PMC6925999
doi:

Substances chimiques

CusB protein, E coli 0
CusC protein, E coli 0
Escherichia coli Proteins 0
Membrane Proteins 0
Membrane Transport Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

25462-25467

Subventions

Organisme : NIAID NIH HHS
ID : F31 AI143208
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM109993
Pays : United States
Organisme : NIH HHS
ID : S10 OD010605
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008500
Pays : United States

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Lauren A Genova (LA)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Melanie F Roberts (MF)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Yu-Chern Wong (YC)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Christine E Harper (CE)

Meinig School of Biomedical Engineering, Cornell University, Ithaca, NY 14853.

Ace George Santiago (AG)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Bing Fu (B)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Abhishek Srivastava (A)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Won Jung (W)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Lucy M Wang (LM)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Łukasz Krzemiński (Ł)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Xianwen Mao (X)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.

Xuanhao Sun (X)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Chung-Yuen Hui (CY)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853.

Peng Chen (P)

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853; pc252@cornell.edu cjh275@cornell.edu.

Christopher J Hernandez (CJ)

Sibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY 14853; pc252@cornell.edu cjh275@cornell.edu.
Meinig School of Biomedical Engineering, Cornell University, Ithaca, NY 14853.

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Classifications MeSH