Document Detail

FabH selectivity for anteiso branched-chain fatty acid precursors in low-temperature adaptation in Listeria monocytogenes.
MedLine Citation:
PMID:  19863661     Owner:  NLM     Status:  MEDLINE    
Gram-positive bacteria, including Listeria monocytogenes, adjust membrane fluidity by shortening the fatty acid chain length and increasing the proportional production of anteiso fatty acids at lower growth temperatures. The first condensation reaction in fatty acid biosynthesis is carried out by beta-ketoacyl-acyl carrier protein synthase III (FabH), which determines the type of fatty acid produced in bacteria. Here, we measured the initial rates of FabH-catalyzed condensation of malonyl-acyl carrier protein and alternate branched-chain precursor acyl-CoAs utilizing affinity-purified His-tagged L. monocytogenes FabH heterologously expressed in Escherichia coli. Listeria monocytogenes FabH showed a preference for 2-methylbutyryl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees C, which was further increased at a low temperature (10 degrees C), suggesting that temperature-dependent substrate selectivity of FabH underlies the increased formation of anteiso branched-chain fatty acids during low-temperature adaptation. The increased FabH preferential condensation of 2-methylbutyryl-CoA could not be attributed to a significantly higher availability of this fatty acid precursor as acyl-CoA pool levels were reduced similarly for all fatty acid precursors at low temperatures.
Atul K Singh; Yong-Mei Zhang; Kun Zhu; Chitra Subramanian; Zhong Li; Radheshyam K Jayaswal; Craig Gatto; Charles O Rock; Brian J Wilkinson
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2009-10-07
Journal Detail:
Title:  FEMS microbiology letters     Volume:  301     ISSN:  1574-6968     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2010-02-05     Completed Date:  2010-04-14     Revised Date:  2013-05-31    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  188-92     Citation Subset:  IM    
Microbiology Group, School of Biological Sciences, Illinois State University, Normal, IL 61790-4120, USA.
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MeSH Terms
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / genetics,  metabolism*
Adaptation, Physiological*
Bacterial Proteins / genetics,  metabolism
Cell Membrane / metabolism*,  physiology
Cold Temperature*
Escherichia coli / genetics,  metabolism
Fatty Acids / metabolism*
Listeria monocytogenes / enzymology,  metabolism,  physiology*
Membrane Fluidity*
Recombinant Proteins / genetics,  metabolism
Substrate Specificity
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Fatty Acids; 0/Recombinant Proteins; EC Synthase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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