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Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase by Filetici, Patrizia; Martegani, Marco Paolo; Valenzuela, Lourdes; González, Alicia; Ballario, Paola is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Glutamate synthase (GOGAT) and glutamine synthetase play a crucial role in ammonium assimilation and glutamate biosynthesis in the yeast Succharomyces cerevisiae. The GOGAT enzyme has been purified and the GOGAT structural gene ( G L T l ) has been cloned, showing that this enzyme is a homotrimeric protein with a monomeric size of 199 kDa. We report the GLTl 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 Eschericlziu coli. Medicago sutiva (alfalfa) and Zra muis (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 GLTl has been deposited in the EMBL data library under Accession Number X89221.

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Author

Filetici, Patrizia; Martegani, Marco Paolo; Valenzuela, Lourdes; González, Alicia; Ballario, Paola

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); John Wiley & Sons Inc.; [Chichester]; [New York]: John Wiley & Sons, ©1985-; Wiley; Hindawi Limited (ISSN 0749-503X)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)