Physiological Role of Acyl Coenzyme A Synthetase Homologs in Lipid Metabolism in Neurospora crassa

Author:

Roche Christine M.12,Blanch Harvey W.12,Clark Douglas S.12,Glass N. Louise23

Affiliation:

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

2. Energy Biosciences Institute, The University of California, Berkeley, California, USA

3. Plant and Microbial Biology Department, The University of California, Berkeley, California, USA

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,General Medicine,Microbiology

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