Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis
Document Type
Article
Publication Title
Journal of Bacteriology
Abstract
The LipB octanoyltransferase catalyzes the first step of lipoic acid synthesis in Escherichia coli, transfer of the octanoyl moiety from octanoyl-acyl carrier protein to the lipoyl domains of the E2 subunits of the 2-oxoacid dehydrogenases of aerobic metabolism. Strains containing null mutations in lipB are auxotrophic for either lipoic acid or octanoic acid. We report the isolation of two spontaneously arising mutant strains that allow growth of lipB strains on glucose minimal medium; we determined that suppression was caused by single missense mutations within the coding sequence of the gene (lplA) that encodes lipoate-protein ligase. The LplA proteins encoded by the mutant genes have reduced Km values for free octanoic acid and thus are able to scavenge cytosolic octanoic acid for octanoylation of lipoyl domains. Copyright © 2009, American Society for Microbiology. All Rights Reserved.
First Page
6796
Last Page
6803
DOI
10.1128/JB.00798-09
Publication Date
11-1-2009
Recommended Citation
Hermes, Fatemah A.M. and Cronan, John E., "Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis" (2009). Basic Sciences Faculty Publications. 116.
https://doi.org/10.1128/JB.00798-09
https://collections.uhsp.edu/basic-sciences_pubs/116