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PMID: 8756637 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Two zinc-finger-containing repressors are responsible for glucose repression of SUC2 expression.

Molecular and cellular biology ·Vol. 16 ·No. 9 ·1996-09-00 ·Pages 4790-7

Lutfiyya LL, Johnston M

Abstract

Expression of the SUC2 gene in Saccharomyces cerevisiae, which encodes invertase, is repressed about 200-fold by high levels of glucose. Mig1p is a Cys2His2 zinc-finger-containing protein required for glucose repression of SUC2 and several other genes. However, SUC2 expression is still about 13-fold repressed by glucose in a mig1 mutant. We have identified a second repressor, Mig2p, containing zinc fingers very similar to those of Mig1p that is responsible for this remaining glucose repression of SUC2 expression. Overexpression of MIG2 represses SUC2 under nonrepressing conditions, and a LexA-Mig2p fusion represses transcription of a lexO-containing promoter in a glucose-dependent manner, supporting the idea that Mig2p is a glucose-activated repressor. We have shown that Mig2p binds to the Miglp-binding sites in the SUC2 promoter. Even though Mig1p and Mig2p bind to similar sites and share almost identical zinc fingers, they differ in their relative affinities for various Mig1p-binding sites. This could explain our observation that MIG2 appears to have little role in glucose repression of other promoters with MIG1-binding sites.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/metabolism Base Sequence Binding Sites DNA-Binding Proteins/physiology Enzyme Induction/drug effects Gene Expression Regulation, Fungal/drug effects Glucose/pharmacology Glycoside Hydrolases/biosynthesis,genetics Molecular Sequence Data Promoter Regions, Genetic Recombinant Fusion Proteins/metabolism Repressor Proteins/genetics,physiology Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Amino Acid Serine Endopeptidases/metabolism Zinc Fingers/physiology beta-Fructofuranosidase
Chemicals
Bacterial Proteins DNA-Binding Proteins LexA protein, Bacteria MIG1 protein, S cerevisiae Recombinant Fusion Proteins Repressor Proteins Saccharomyces cerevisiae Proteins Glycoside Hydrolases beta-Fructofuranosidase Serine Endopeptidases Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lutfiyya L L
Department of Genetics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Johnston M
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32 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1996-09-00
Pages
4790-7
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC231480
Subset
IM
Grants
NIGMS NIH HHS · R01 GM032540 · United States
NIGMS NIH HHS · GM32540 · United States
Databases
GENBANK
U18778, U54564
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