Open AccessLipid composition of cAMP‐dependent protein kinase mutants of Aspergillus niger
Author(s) -
Jernejc Katarina,
Benčina Mojca
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00532-9
Subject(s) - lysophosphatidylethanolamine , phosphatidylethanolamine , biochemistry , protein subunit , lipase , phosphatidylcholine , aspergillus niger , mutant , protein kinase a , phosphatidylinositol , biology , chemistry , enzyme , kinase , phospholipid , gene , membrane
Lipid composition of cAMP‐dependent protein kinase (PKA) Aspergillus niger mutants with overexpressed or deleted genes for either regulatory and/or the catalytic subunit of PKA was analyzed. Disruption of the gene encoding the PKA regulatory subunit resulted in 20% less total lipids, 30% less neutral lipids, four times more glycolipids and two‐fold higher triacylglycerol lipase activity compared to the control strain. Concomitantly a five‐fold decrease in phosphatidylcholine, accompanied with 1.5‐, 1.8‐ and 2.8‐fold increases in phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylinositol, was determined, respectively. The lack of PKA activity, due to the disruption of a gene encoding the PKA catalytic subunit, resulted in a 1.6‐times increase in total lipids with two times more neutral lipids associated with lower triacylglycerol lipase activity and a decrease in phospholipids. The mutants with unrestricted PKA activity synthesized twice as much citric acid as the control strain and three times more than strains lacking PKA activity. The results indicate the involvement of cAMP‐mediated PKA activity in regulation of lipid biosynthesis as well as citric acid synthesis.