Genetic and Enzymatic Characterization of the Inducible Glycerol Dissimilatory System of Neurospora Crassa

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1982 Aug 1

PMID 6284716

Citations 1

Authors

P F Denor

J B Courtright

Affiliations

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Abstract

The glycerol dissimilatory system in Neurospora crassa was analyzed through the characterization of 18 Glp- mutants which were isolated after inositol-less death and filtration enrichment. All mutants obtained by this procedure could be assigned to one of three complementation groups. The subsequent genetic characterization of these glp mutations revealed lesions on the I, II, and VI chromosomes at the glp-1, glp-2, and glp-4 loci, each of which was subjected to fine-structure analysis. Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively. Additional evidence, obtained from studies of the inducibility of glycerokinase by glycerol, cold treatment, or deoxyribose, suggests that glp-1 is involved in controlling the expression of glp-4.

Citing Articles

Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress.

Luyten K, Albertyn J, Skibbe W, Prior B, Ramos J, Thevelein J EMBO J. 1995; 14(7):1360-71.

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