Azf1p is a nuclear-localized zinc-finger protein that is preferentially expressed under non-fermentative growth conditions in Saccharomyces cerevisiae

1998 ◽  
Vol 34 (4) ◽  
pp. 287-296 ◽  
Author(s):  
Torsten Stein ◽  
Jörn Kricke ◽  
Dietmar Becher ◽  
T. Lisowsky
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Growth Conditions ◽  
Finger Protein ◽  
Fermentative Growth

Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae

1993 ◽  
Vol 13 (7) ◽  
pp. 3872-3881
Author(s):  
F Estruch ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Wilms Tumor ◽  
Temperature Sensitive ◽  
Carbon Utilization ◽  
Functional Roles ◽  
Multicopy Suppressor ◽  
Finger Protein

The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong transcriptional activators when bound to DNA. Functional roles of this zinc finger protein family are discussed.

scholarly journals Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae.

1993 ◽  
Vol 13 (7) ◽  
pp. 3872-3881 ◽  
Author(s):  
F Estruch ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Wilms Tumor ◽  
Temperature Sensitive ◽  
Carbon Utilization ◽  
Functional Roles ◽  
Multicopy Suppressor ◽  
Finger Protein

The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong transcriptional activators when bound to DNA. Functional roles of this zinc finger protein family are discussed.

scholarly journals Yeast PalA/AIP1/Alix Homolog Rim20p Associates with a PEST-Like Region and Is Required for Its Proteolytic Cleavage

2001 ◽  
Vol 183 (23) ◽  
pp. 6917-6923 ◽  
Author(s):  
Wenjie Xu ◽  
Aaron P. Mitchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Candida Albicans ◽  
Zinc Finger ◽  
Cysteine Protease ◽  
Zinc Finger Protein ◽  
Mutant Proteins ◽  
Finger Protein ◽  
Genome Wide ◽  
Close Proximity ◽  
Two Hybrid

ABSTRACT The Saccharomyces cerevisiae zinc finger protein Rim101p is activated by cleavage of its C-terminal region, which resembles PEST regions that confer susceptibility to proteolysis. Here we report that Rim20p, a member of the broadly conserved PalA/AIP1/Alix family, is required for Rim101p cleavage. Two-hybrid and coimmunoprecipitation assays indicate that Rim20p binds to Rim101p, and a two-hybrid assay shows that the Rim101p PEST-like region is sufficient for Rim20p binding. Rim101p-Rim20p interaction is conserved in Candida albicans, supporting the idea that interaction is functionally significant. Analysis of Rim20p mutant proteins indicates that some of its broadly conserved regions are required for processing of Rim101p and for stability of Rim20p itself but are not required for interaction with Rim101p. A recent genome-wide two-hybrid study (T. Ito, T. Chiba, R. Ozawa, M. Yoshida, M. Hattori, and Y. Sakaki, Proc. Natl. Acad. Sci. USA 98:4569–4574, 2000) indicates that Rim20p interacts with Snf7p and that Snf7p interacts with Rim13p, a cysteine protease required for Rim101p proteolysis. We suggest that Rim20p may serve as part of a scaffold that places Rim101p and Rim13p in close proximity.

scholarly journals Identification and Analysis of Mot3, a Zinc Finger Protein That Binds to the Retrotransposon Ty Long Terminal Repeat (δ) in Saccharomyces cerevisiae

1998 ◽  
Vol 18 (4) ◽  
pp. 1879-1890 ◽  
Author(s):  
Jon M. Madison ◽  
Aimée M. Dudley ◽  
Fred Winston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Long Terminal Repeat ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Independent Study ◽  
Terminal Repeat ◽  
Mrna Levels ◽  
Finger Protein ◽  
Partial Suppression

ABSTRACT Spt3 and Mot1 are two transcription factors of Saccharomyces cerevisiae that are thought to act in a related fashion to control the function of TATA-binding protein (TBP). Current models suggest that while Spt3 and Mot1 do not directly interact, they do function in a related fashion to stabilize the TBP-TATA interaction at particular promoters. Consistent with this model, certain combinations of spt3 and mot1 mutations are inviable. To identify additional proteins related to Spt3 and Mot1 functions, we screened for high-copy-number suppressors of the mot1 spt3inviability. This screen identified a previously unstudied gene,MOT3, that encodes a zinc finger protein. We show that Mot3 binds in vitro to three sites within the retrotransposon Ty long terminal repeat (δ) sequence. One of these sites is immediately 5′ of the δ TATA region. Although a mot3 null mutation causes no strong phenotypes, it does cause some mild phenotypes, including a very modest increase in Ty mRNA levels, partial suppression of transcriptional defects caused by a mot1 mutation, and partial suppression of an spt3 mutation. These results, in conjunction with those of an independent study of Mot3 (A. Grishin, M. Rothenberg, M. A. Downs, and K. J. Blumer, Genetics, in press), suggest that this protein plays a varied role in gene expression that may be largely redundant with other factors.

Sign in / Sign up

Export Citation Format

Share Document