By Robert K. Poole
First released in 1967, Advances in Microbial body structure is considered one of Elsevier's most famous and acclaimed sequence. Now edited via Professor Robert Poole, collage of Sheffield, Advances in Microbial body structure keeps to put up topical and significant experiences, examining body structure in its broadest context, to incorporate all fabric that contributes to our realizing of ways microorganisms and their part components paintings. issues contain: * Glutathione, Altruistic Metabolite in Fungi * The position of the Flavodiiron Proteins in Microbial Nitric Oxide detoxing * rigidity Responsive micro organism: Biosensors as Environmental displays * Bacterial Na+ -or H+ - coupled ATP working at low electrochemical capability * Dissimiatory Fe(III) and Mn(IV) aid
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Extra info for Advances in Microbial Physiology, Vol. 49
K. (2000) Hgt1p, a high aﬃnity glutathione transporter from the yeast Saccharomyces cerevisiae. J. Biol. Chem. 275, 13259–13265. , Melki, R. and Morera, S. (2001) Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40, 13564–13573. Boyland, E. F. (1969) The role of glutathione and glutathione Stransferases in mercapturic acid biosynthesis. Adv. Enzymol. Relat. Areas. Mol. Biol. 32, 173–219. , Clemens, S. -J. 1 |, direct submission to database.
Degradation of GSH remains unknown in yeast and fungi. Part B. The glutathione–glutaredoxin–thioredoxin system in fungi. The oxidized disulﬁde form of thioredoxin (TRX2) is reduced directly by NADPH and thioredoxin reductase (TRR1). Oxidized glutaredoxin, glutathionedependent oxidoreductase (GRX1 and GRX2) is reduced by GSH and oxidized GSSG is reduced by NADP-dependent glutathione reductase (GLR1). Thioredoxins act as hydrogen donors for PAPS reductase (MET16) and thioredoxin peroxidases (TSA1, AHP1 and YDR453/YBL064c) and both thioredoxins and glutaredoxins act as hydrogen donors for ribonucleotide reductase in yeast and fungi.
Biol. 23, 163–177. A. -J. (2002) A second stress-inducible glutathione S-transferase gene from Schizosaccharomyces pombe. Biochim. Biophys. Acta 1574, 399–402. , Lou, W. and Vancura, A. (1998) A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273, 29915–29922. , Neumann, D. I. (1999) Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast. EMBO J. 18, 3325–3333. Cobbett, C.