Inhibition of cardiolipin biosynthesis partially suppresses the sensitivity of an Escherichia coli mutant lacking OmpC to envelope stress

Porins in the outer membrane (OM) of Gram-negative bacteria play two main functions: passage of various extracellular molecules and maintenance of membrane integrity. OmpC, a non-specific porin, is involved in both functions; however, the exact mechanism of maintenance of membrane integrity remains...

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Bibliographic Details
Published in:The journal of microbiology Vol. 63; no. 11; p. e2507004
Main Authors: Ryu, Dae-Beom, Choi, Umji, Han, Gyubin, Lee, Chang-Ro
Format: Journal Article
Language:English
Published: Korea (South) 한국미생물학회 01.11.2025
Subjects:
Bacterial Outer Membrane - metabolism
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Cardiolipins - biosynthesis
Cell Membrane - metabolism
Escherichia coli - genetics
Escherichia coli - growth & development
Escherichia coli - metabolism
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Mutation
Porins - genetics
Porins - metabolism
Stress, Physiological
생물학
YhdP
membrane integrity
phospholipid transport
porins
OmpC
cardiolipin
ISSN:1976-3794, 1225-8873, 1976-3794
Online Access:Get full text
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Summary:Porins in the outer membrane (OM) of Gram-negative bacteria play two main functions: passage of various extracellular molecules and maintenance of membrane integrity. OmpC, a non-specific porin, is involved in both functions; however, the exact mechanism of maintenance of membrane integrity remains unknown. In this study, we found that inhibiting cardiolipin biosynthesis partially restored the growth defect of the ompC mutant under envelope stress. Among the three enzymes involved in cardiolipin biosynthesis, ClsABC, this effect is primarily associated with ClsA. Notably, the deletion of ClsA also suppressed the similar phenotypes of an Escherichia coli mutant lacking YhdP, a transmembrane protein involved in phospholipid transport from the inner membrane to the OM. Collectively, these results imply that OmpC may contribute to membrane integrity, partially through mechanisms linked to transport or biosynthesis of phospholipids such as cardiolipin.
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ISSN:1976-3794
1225-8873
1976-3794
DOI:10.71150/jm.2507004