Effects of three mutant genes, CAT1-2d, cat2-1 and hex2-3, on catabolite repression of mitochondrial cytochromes and the first two enzymes of haem biosynthesis were compared. The CAT1-2d mutation gave no resistance to glucose, whereas cat2-1 endowed both cytochromes and 5-aminolaevulinate dehydratase with resistance, but did not alter the effect of glucose on 5-aminolaevulinate synthase. The hex2-3 mutation caused repression resistance of cytochromes and of the two haem biosynthetic enzymes. hex2-3 strains also accumulated intracellular 5-aminolaevulinate. Co-inheritance of the latter traits, sensitivity to maltose inhibition and ability to grow on raffinose in the presence of 2-deoxyglucose, demonstrated that the pleiotropic phenotype is a function of the single gene hex2-3. Revertants which grew on maltose regained sensitivity to deoxyglucose and exhibited normal sensitivity of cytochromes and haem biosynthesis enzymes to repression. Addition of the hex1-18 mutation, which renders cytochromes resistant to repression, to a cat2-1 strain did not produce the same effect on 5-aminolaevulinate synthase as hex2-3. It is concluded that repression patterns of haem and cytochrome biosynthesis are substantially affected by hex2-3 and cat2-1 but not by CAT1-2d.
ArreseM.,
CarvajalE.,
RobisonS.,
SambunarisA.,
PanekA.,
MattoonJ.1983; Cloning of the β-aminolevulinic acid synthase structural gene in yeast. Current Genetics 7:175–183
BaileyR.B.,
WoodwardA.1984; Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae
. Molecular and General Genetics 193:507–512
BorralhoL.M.,
PanekA.D.,
MalamudD.R.,
SandersH.K.,
MattoonJ.R.1983; In situ assay for 5-aminolevulinate dehydratase and application to the study of a catabolite repression- resistant Saccharomyces cerevisiae mutant. Journal of Bacteriology 156:141–147
EntianK.-D.1977; Lack of carbon catabolite inactivation in a mutant of Saccharomyces cerevisiae with reduced hexokinase activity. Molecular and General Genetics 158:201–210
EntianK.-D.1980; A defect in carbon catabolite repression associated with uncontrollable and excessive maltose uptake. Molecular and General Genetics 179:169–175
EntianK.-D.,
ZimmermannF.K.1980; Glycoltic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae
. Molecular and General Genetics 177:345–350
EntianK.-D.,
ZimmermannF.K.,
ScheelI.1977; A partial defect in carbon catabolite repression in mutants of Saccharomyces cerevisiae with reduced hexose phosphorylation. Molecular and General Genetics 156:99–105
GancedoJ.M.,
GancedoC.1971; Fructose-1,6- diphosphatase, phosphofructokinase and glucose-6- phosphate dehydrogenase from fermenting and nonfermenting yeasts. Archives of Microbiology 76:132–138
Labbe-BoisR.,
VollandC.1977; Changes in the, activities of the protoheme-synthesizing systems during growth of yeast under different conditions. Archives of Biochemistry and Biophysics 179:565–577
MahlerH.R.,
LinC.C.1978; Exogenous adenosine 3',5'-monophosphate can release yeast from catabolite repression. Biochemical and Biophysical Research Communications 83:1039–1047
MalamudD.R.,
BorralhoL.M.,
PanekA.D.,
MattoonJ.R.1979; Modulation of cytochrome biosynthesis in yeast by antimetabolite action of levulinic acid. Journal of Bacteriology 138:799–804
MalamudD.R.,
PadraoG.R.B.,
BorralhoL.,
ArreseM.,
PanekA.D.,
MattoonJ.R.1983; Regulation of porphyrin biosynthesis in yeast. Use of 5-aminolevulinic acid in characterizing in vivo effects of mutation. Brazilian Journal of Medical and Biological Research 16:203–213
MatsumotoK.,
UnoI.,
Toh-EA.,
IshikawaT.,
OshimaY.1982; Cyclic AMP may not be involved in catabolite repression in Saccharomyces cerevisiae. Evidence from mutants capable of utilizing it as an adenine source. Journal of Bacteriology 150:277–285
MattoonJ.R.,
MalamudD.R.,
BrunnerA.,
BrazG.,
CarvajalE.,
LancashireW.E.,
PanekA.D.1978; Regulation of heme formation and cytochrome biosynthesis in normal and mutant yeasts. In Biochemistry and Genetics of Yeast, Pure and Applied Aspects pp. 145–160BacilaM.,
HoreckerB.,
StoppaniA. O.M.
Edited by New York: Academic Press;
MattoonJ.R.,
LancashireW.E.,
SandersH.K.,
CarvajalE.,
MalamudD.R.,
BrazG.R.C.,
PanekA.D.1979; Oxygen and catabolite regulation of hemoprotein biosynthesis in yeast. In Biochemical and Clinical Aspects of Oxygen pp.
CaugheyW.
Edited by New York: Academic Press;
MauzerallD.,
GranickS.1956; The occurrence and determination of 5-aminolevulinic acid and porphobilinogen in urine. Journal of Biological Chemistry 219:435–446
MichelsC.A.,
HahnenbergerK.M.,
SylvestreY.1983; Pleiotropic mutations regulating resistance to glucose repression in Saccharomyces carlsbergensis are allelic to the structural gene for hexokinase B. Journal of Bacteriology 153:574–578
PaschoalinV.M.F.,
Costa-CarvalhoV.L.A.,
PanekA.D.1986; Further evidence for the alternative pathway of trehalose synthesis linked to maltose utilization in Saccharomyces
. Current Genetics 10:725–731
PerlmanP.S.,
MahlerH.R.1974; Derepression of mitochondria and their enzymes in yeast: regulatory aspects. Archives of Biochemistry and Biophysics 162:248–271
PolakisE.S.,
BartleyW.1965; Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources. Biochemical Journal 97:284–297
Van RijnJ.,
Van WijkR.1972; Differential sensitivities of the two malate dehydrogenases and the maltose permease to the effect of glucose in Saccharomyces carlsbergensis
. Journal of Bacteriology 110:477–484
ZimmermannF.K.,
KaufmannI.,
RasenbergerH.,
HaussmanP.1977; Genetics of carbon catabolite repression in Saccharomyces cerevisiae: genes involved in the derepression process. Molecular and General Genetics 151:95–103
ZimmermannF.K.,
EatonN.R.1974; Genetics of induction and catabolite repression of maltase synthesis in Saccharomyces cerevisiae
. Molecular and General Genetics 134:261–272