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Isolation and primary structure of the gene encoding fructose‐1,6‐bisphosphatase from Saccharomyces cerevisiae
Author(s) -
Entian Karl-Dieter,
Vogel Rudi F.,
Rose Matthias,
Hofmann Lucia,
Mecke Dieter
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80313-2
Subject(s) - saccharomyces cerevisiae , gene , homology (biology) , mutant , fructose 1,6 bisphosphatase , microbiology and biotechnology , biology , transformation (genetics) , protein primary structure , biochemistry , dna , peptide sequence , enzyme
The gene encoding Saccharomyces cerevisiae fructose‐1,6‐bisphosphatase ( FBP1 ) was isolated. Constructed fbpi::HIS3 null mutants were unable to grow with ethanol, and growth was restored after transformation with the cloned fbp gene. The gene codes for a protein of 347 amino acid residues with an M r of 38131. Homology with the pig kidney cortex and the sheep liver enzyme is 47.7% and 46.6%, respectively, within a central core of 328 amino acid residues. The cloned promoter size was 318 bp and allowed only low level expression of the gene. This indicates a positive activation site (UAS) upstream of the cloned DNA fragment.