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Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase
Author(s) -
Heinisch Jürgen J.,
Müller Susanne,
Schlüter Elke,
Jacoby Jörg,
Rodicio Rosaura
Publication year - 1998
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(199802)14:3<203::aid-yea205>3.0.co;2-8
Subject(s) - biology , phosphoglycerate mutase , gene , yeast , genetics , promoter , mutant , mutase , gene duplication , isozyme , genome , enzyme , biochemistry , gene expression , glycolysis
Our previous data indicated that GPM1 encodes the only functional phosphoglycerate mutase in yeast. However, in the course of the yeast genome sequencing project, two homologous sequences, designated GPM2 and GPM3 , were detected. They have been further investigated in this work. Key residues in the deduced amino acid sequence, shown to be involved in catalysis for Gpm1 (i.e. His8, Arg59, His181) are conserved in both enzymes. Overexpression of the genes under control of their own promoters in a gpm1 deletion mutant did not complement for any of the phenotypes. This could in part be attributed to a lack of expression due to their weak promoters. Higher level expression under the control of the yeast PFK2 promoter partially complemented the gpm1 defects, without restoring detectable enzymatic activity. Nevertheless, deletion of either GPM2 or GPM3 , or the two deletions in concert, did not produce any obvious lesions for growth on a variety of different carbon sources, nor did they change the levels of key intermediary metabolites. We conclude that both genes evolved from duplication events and that they probably constitute non‐functional homologues in yeast.