The Unusual Substrate Specificity of Escherichia coli Cardiolipin Synthase C Does Not Require the Product of the Transcriptionally Engaged ymdB Gene

Authors

Katsuhiro Sawasato
Mikhail Bogdanov

Publication Date

6-1-2024

Journal

BBA Molecular and Cell Biology of Lipids

Abstract

Polycistronic transcription and translation of ymdB-clsC have been thought to be required for full activity of ClsC. The authentic initiation codon of the clsC gene is present within the open reading frame of the upstream located ymdB gene. ClsC translated from authentic initiation codon drives cardiolipin (CL) synthesis without transcriptionally paired YmdB. YmdB is not necessary for the substrate specificity of ClsC utilizing phosphatidylethanolamine (PE) as a co-substrate.

Keywords

Cardiolipins, Escherichia coli, Escherichia coli Proteins, Membrane Proteins, Phosphatidylethanolamines, Substrate Specificity, Transcription, Genetic, Transferases (Other Substituted Phosphate Groups), Cardiolipin, Cardiolipin synthase C, clsC, Translation initiation codon, Polycistronic operon, Gene regulation

DOI

10.1016/j.bbalip.2024.159483

PMID

38527666

PMCID

PMC11678504

PubMedCentral® Posted Date

12-27-2024

PubMedCentral® Full Text Version

Author MSS

Published Open-Access

yes