Loss of phosphatidylserine synthesis results in aberrant solute sequestration and vacuolar morphology in Saccharomyces cerevisiae.
Null cho1 mutants of Saccharomyces cerevisiae are incapable of phosphatidyl-serine synthesis. They were more susceptible than wild-type strains to 100 mM CaCl2, 3 mM ZnCl2 or 1 mM MnCl2, but not to MgCl2 nor KCl. They were also susceptible to high concentrations of basic amino acids, L-lysine and L-arginine, and to an L-lysine analog, S-2-aminoethyl-L-cysteine. Their vacuolar pools of amino acids, especially those of basic ones, were decreased. Pigmentation of cho1 ade2 double mutants was obscured and vacuoles of cho1 mutants were considerably fragmented. These indicate that phosphatidylserine plays vital roles in normal vacuolar function and morphogenesis.
Department of Biochemistry, Saitama University, Japan.
S
S
Hamamatsu
I
I
Shibuya
M
M
Takagi
A
A
Ohta
D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase / Q000235:genetics / Q000378:metabolism; D002262:Carboxy-Lyases / Q000235:genetics; D002413:Cations, Divalent / Q000494:pharmacology; D009154:Mutation; D010718:Phosphatidylserines / Q000096:biosynthesis / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000502:physiology*; D014617:Vacuoles / Q000502:physiology*
D002413:Cations, Divalent; D010718:Phosphatidylserines; D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase; D002262:Carboxy-Lyases; C022378:phosphoribosylaminoimidazole carboxylase