Molecular genetics of superoxide dismutases in yeasts and related fungi.

作者: Edith Butler Gralla , Daniel J. Kosman

DOI: 10.1016/S0065-2660(08)60322-3

关键词: YeastEnzymeSuperoxideExtracellularGeneBiochemistryBiologySaccharomyces cerevisiaeGene expressionSuperoxide dismutase

摘要: Publisher Summary This chapter discusses the molecular genetics of superoxide dismutases in yeasts and related fungi. The provides information on various enzymes that are responsible for establishing themselves as first component defense mechanism, such dismutases. These catalyze disproportionation O2-, to H2O2 O2. As discussed chapter, eukaryotes contain at least two catalytically equivalent but evolutionarily, genetically, structurally distinct. Superoxide can be produced a wide variety cellular redox processes. simple type reaction generate O2- is auto-oxidation. In Saccharomyces cerevisiae, dominant source appears leakage from mitochondrial electron transport chain. also functionally distinct because these found different cell compartments. regulation expression along with discussion their physiologic functions light phenotypes strains yeast fungi lack either or both activities. addition enzymes, an extracellular Cu,ZnSOD characterized eukaryotes. human enzyme, designated ECSOD1, secreted glycoprotein containing Cu Zn; gene this SOD has been cloned. Although ECSOD intracellular SODl differ primary sequence, they share number structural homologies respect metal centers. Some evidences dismutase S. cerevisiae N. crassa presented chapter.

参考文章(178)
J. Welch, S. Fogel, C. Buchman, M. Karin, The CUP2 gene product regulates the expression of the CUP1 gene, coding for yeast metallothionein. The EMBO Journal. ,vol. 8, pp. 255- 260 ,(1989) , 10.1002/J.1460-2075.1989.TB03371.X
T. Belazzi, A. Wagner, R. Wieser, M. Schanz, G. Adam, A. Hartig, H. Ruis, Negative regulation of transcription of the Saccharomyces cerevisiae catalase T (CTT1) gene by cAMP is mediated by a positive control element. The EMBO Journal. ,vol. 10, pp. 585- 592 ,(1991) , 10.1002/J.1460-2075.1991.TB07985.X
K Lerch, E Schenk, Primary structure of copper-zinc superoxide dismutase from Neurospora crassa. Journal of Biological Chemistry. ,vol. 260, pp. 9559- 9566 ,(1985) , 10.1016/S0021-9258(17)39271-2
Elizabeth W. Jones, Gerald R. Fink, Regulation of Amino Acid and Nucleotide Biosynthesis in Yeast Cold Spring Harbor Monograph Archive. ,vol. 11, pp. 181- 299 ,(1982) , 10.1101/087969180.11B.181
Alberto Boveris, PRODUCTION OF SUPEROXIDE ANION AND HYDROGEN PEROXIDE IN YEAST MITOCHONDRIA Biochemistry and Genetics of Yeast#R##N#Pure and Applied Aspect. pp. 65- 80 ,(1978) , 10.1016/B978-0-12-071250-2.50010-0
Joel S. Levine, The origin and evolution of atmospheric oxygen. Progress in Clinical and Biological Research. ,vol. 274, pp. 111- ,(1988)
M. Brunori, G. Rotilio, Biochemistry of oxygen radical species. Methods in Enzymology. ,vol. 105, pp. 22- 35 ,(1984) , 10.1016/S0076-6879(84)05005-9
Kenneth D. Munkres, [24] Purification of exocellular superoxide dismutases Methods in Enzymology. ,vol. 186, pp. 249- 260 ,(1990) , 10.1016/0076-6879(90)86116-D