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Eukaryot Cell. 2013 Sep;12(9):1244-57. doi: 10.1128/EC.00079-13. Epub 2013 Jul 19.

Physiological role of Acyl coenzyme A synthetase homologs in lipid metabolism in Neurospora crassa.

Author information

1
Chemical and Biomolecular Engineering Department, The University of California, Berkeley, California, USA.

Abstract

Acyl coenzyme A (CoA) synthetase (ACS) enzymes catalyze the activation of free fatty acids (FAs) to CoA esters by a two-step thioesterification reaction. Activated FAs participate in a variety of anabolic and catabolic lipid metabolic pathways, including de novo complex lipid biosynthesis, FA β-oxidation, and lipid membrane remodeling. Analysis of the genome sequence of the filamentous fungus Neurospora crassa identified seven putative fatty ACSs (ACS-1 through ACS-7). ACS-3 was found to be the major activator for exogenous FAs for anabolic lipid metabolic pathways, and consistent with this finding, ACS-3 localized to the endoplasmic reticulum, plasma membrane, and septa. Double-mutant analyses confirmed partial functional redundancy of ACS-2 and ACS-3. ACS-5 was determined to function in siderophore biosynthesis, indicating alternative functions for ACS enzymes in addition to fatty acid metabolism. The N. crassa ACSs involved in activation of FAs for catabolism were not specifically defined, presumably due to functional redundancy of several of ACSs for catabolism of exogenous FAs.

PMID:
23873861
PMCID:
PMC3811560
DOI:
10.1128/EC.00079-13
[Indexed for MEDLINE]
Free PMC Article

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