Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the upstream region in regulation of glutamine synthetase expression
Open Access
- 1 March 1992
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 174 (6) , 1828-1836
- https://doi.org/10.1128/jb.174.6.1828-1836.1992
Abstract
The GLN1 gene, encoding glutamine synthetase in Saccharomyces cerevisiae, was sequenced, and its encoded polypeptide was shown to have significant homology to other eukaryotic glutamine synthetases. S1 analysis has defined the transcriptional start site of the gene. Upstream analysis of the gene using lacZ fusions has verified transcriptional control of the gene and has identified a nitrogen upstream activation sequence which is required for the increased transcription of GLN1 seen when glutamine is replaced by glutamate as the nitrogen source. cis-acting sites required for the increased transcription in response to purine starvation also have been localized.Keywords
This publication has 32 references indexed in Scilit:
- A rapid boiling method for the preparation of bacterial plasmidsPublished by Elsevier ,2004
- A mechanism for synergistic activation of a mammalian gene by GAL4 derivativesNature, 1990
- How different eukaryotic transcriptional activators can cooperate promiscuouslyNature, 1990
- The erythroid-specific transcription factor eryf1: A new finger proteinCell, 1989
- Heme regulates transcription of the CYC1 gene of S. cerevisiae via an upstream activation siteCell, 1983
- [3] An integrated and simplified approach to cloning into plasmids and single-stranded phagesPublished by Elsevier ,1983
- [13] Eviction and transplacement of mutant genes in yeastPublished by Elsevier ,1983
- [9] Construction and use of gene fusions to lacZ (β-galactosidase) that are expressed in yeastPublished by Elsevier ,1983
- Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of S1 endonuclease-digested hybridsCell, 1977
- Yeast mutants pleiotropically impaired in the regulation of the two glutamate dehydrogenasesBiochemical and Biophysical Research Communications, 1973