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Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase
Author(s) -
Filetici Patrizia,
Martegani Marco Paolo,
Valenzuela Lourdes,
González Alicia,
Ballario Paola
Publication year - 1996
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(199610)12:13<1359::aid-yea3>3.0.co;2-5
Subject(s) - biology , biochemistry , saccharomyces cerevisiae , glutamate synthase , glutamine synthetase , peptide sequence , nucleic acid sequence , amino acid , yeast , gene , glutamine
Glutamate synthase (GOGAT) and glutamine synthetase play a crucial role in ammonium assimilation and glutamate biosynthesis in the yeast Saccharomyces cerevisiae . The GOGAT enzyme has been purified and the GOGAT structural gene ( GLT1 ) has been cloned, showing that this enzyme is a homotrimeric protein with a monomeric size of 199kDa. We report the GLT1 nucleotide sequence and the amino acid sequence of its deduced protein product. Our results show that there is a high conservation with the corresponding genes of Escherichia coli, Medicago sativa (alfalfa) and Zea mais (maize). Binding domains for glutamine, cofactors (FMN and NADH) and the cysteine clusters (which comprise the iron‐sulfur centres) were tentatively identified on the basis of sequence comparison with GOGAT sequences from E. coli , alfalfa and maize. The sequence of GLT1 has been deposited in the EMBL data library under Accession Number X89221.