Disease relevance of FAA1

• Very long chain acyl-CoA synthetase activity is reduced in strains containing a disrupted FAT1 gene and is increased when FAT1 is expressed in insect cells under control of a baculovirus promoter [1].
• Pcs60p belongs to the family of proteins which act via an ATP-dependent covalent binding of AMP to their substrates and shows the highest degree of similarity to the Escherichia coli long chain acyl-CoA synthetase [2].
• This process is impaired in X-linked adrenoleukodystrophy (XALD) patients as a result of decreased activity of peroxisomal very long-chain acyl-CoA synthetase (VLCS) [3].

High impact information on FAA1

• Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae [4].
• Analyses of strains containing NMT1 and a faal null mutation indicated that FAA1 is not essential for vegetative growth when an active de novo pathway for fatty acid synthesis is present [5].
• The role of FAA1 in cellular lipid metabolism and protein N-myristoylation was therefore assessed in strains subjected to biochemical or genetic blockade of FAS [5].
• This single copy gene, which maps to the right arm of chromosome XV, specifies a long chain acylCoA synthetase of 700 amino acids [5].
• Chromosomally encoded FAA1 and FAT1 are not able to suppress the growth deficiencies of the fat1Delta faa1Delta and faa1Delta faa4Delta strains, respectively, indicating Faa1p and Fat1p play distinct roles in the fatty acid import process [6].

Biological context of FAA1

• The mutation that causes the fatty acid secretion phenotype occurred at a single allele, and this phenotype was suppressed by the introduction of a single copy of FAA1, a gene for acyl-CoA Synthetase, to the mutant [7].
• Fatty acid activation gene (FAA1) in sake yeast Kyokai no [8].
• A novel murine long-chain acyl-CoA synthetase expressed in brain participates in neuronal cell proliferation [9].

Anatomical context of FAA1

• When organelles were fractionated on a sucrose gradient, VLCS activity co-localized with peroxisomes while long chain acyl-CoA synthetase activity associated primarily with mitochondria [3].
• Irreversible deacylation of plasma membrane phospholipids by the combined action of Mg2+ and a long-chain acyl-CoA synthetase inhibitor in Saccharomyces cerevisiae [10].

Associations of FAA1 with chemical compounds

• At 36 degrees C, FAA1 is required for the utilization of exogenous myristate by NMT and for the synthesis of several phospholipid species [5].
• Effect of the FAA1 gene disruption of sake yeast on the accumulation of ethyl caproate in sake mash [8].
• The disruptant for the FAA1 gene (K701deltafaa1) exhibited a reduced growth rate in a medium containing cerulenin and myristic acid or oleic acid compared with that of the parental strain (K701) [8].
• The depression in very long-chain acyl CoA synthetase activities were not apparent in cells grown in the presence of oleate [11].
• A long-chain acyl-CoA synthetase (Faap) inhibitor, adenosine 5'-hexadecylphosphate (AMPC16), caused lethal plasma membrane damage to Saccharomyces cerevisiae cells as reflected by the leakage of cytoplasmic K+ into medium in which Mg2+ was supplemented at 10 mM [10].

Other interactions of FAA1

• Simultaneous disruption of FAA1 and FAA4, which encode long chain (C14-C18) fatty acyl-CoA synthetases, effectively blocks the import of long chain saturated and unsaturated fatty acids [1].
• Two fatty acid activation genes, FAA1 and FAA4, were found to be essential for unsaturated fatty acid repression of OLE1 through the FAR sequences [12].
• Interestingly, the growth defect caused by snc1 overexpression was rescued by the overexpression of FAA4, but not of FAA1, which plays a predominant role in laboratory strains [13].

References