Glucose repression on RIM1 , a gene encoding a mitochondrial single-stranded DNA-binding protein, in Saccharomyces cerevisiae : a possible regulation at pre-mRNA splicing

1998 ◽  
Vol 34 (5) ◽  
pp. 351-359 ◽  
Author(s):  
Zhijun Li ◽  
F. Ling ◽  
T. Shibata
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Glucose Repression ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Mrna Splicing ◽  
Gene Encoding ◽  
Single Stranded Dna

scholarly journals Identification, Cloning, and Characterization of the Bacteriophage N4 Gene Encoding the Single-stranded DNA-binding Protein

1995 ◽  
Vol 270 (38) ◽  
pp. 22541-22547 ◽  
Author(s):  
Mieyoung Choi ◽  
Alita Miller ◽  
Nam-Young Cho ◽  
Lucia B. Rothman-Denes
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Gene Encoding ◽  
Single Stranded Dna ◽  
Bacteriophage N4

scholarly journals A mutation in the gene encoding the Saccharomyces cerevisiae single-stranded DNA-binding protein Rfa1 stimulates a RAD52-independent pathway for direct-repeat recombination.

1995 ◽  
Vol 15 (3) ◽  
pp. 1632-1641 ◽  
Author(s):  
J Smith ◽  
R Rothstein
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Binding Protein ◽  
Large Subunit ◽  
Direct Repeat ◽  
Fold Increase ◽  
Dna Binding Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Single Stranded Dna ◽  
Mutant Strains

In the yeast Saccharomyces cerevisiae, recombination between direct repeats is synergistically reduced in rad1 rad52 double mutants, suggesting that the two genes define alternate recombination pathways. Using a classical genetic approach, we searched for suppressors of the recombination defect in the double mutant. One mutation that restores wild-type levels of recombination was isolated. Cloning by complementation and subsequent physical and genetic analysis revealed that it maps to RAF1. This locus encodes the large subunit of the single-stranded DNA-binding protein complex, RP-A, which is conserved from S. cerevisiae to humans. The rfa1 mutation on its own causes a 15-fold increase in direct-repeat recombination. However, unlike most other hyperrecombination mutations, the elevated levels in rfa1 mutants occur independently of RAD52 function. Additionally, rfa1 mutant strains grow slowly, are UV sensitive, and exhibit decreased levels of heteroallelic recombination. DNA sequence analysis of rfa1 revealed a missense mutation that alters a conserved residue of the protein (aspartic acid 228 to tyrosine [D228Y]). Biochemical analysis suggests that this defect results in decreased levels of RP-A in mutant strains. Overexpression of the mutant subunit completely suppresses the UV sensitivity and partially suppresses the recombination phenotype. We propose that the defective complex fails to interact properly with components of the repair, replication, and recombination machinery. Further, this may permit the bypass of the recombination defect of rad1 rad52 mutants by activating an alternative single-stranded DNA degradation pathway.

scholarly journals Synergistic release from glucose repression by mig1 and ssn mutations in Saccharomyces cerevisiae.

Genetics ◽  
1994 ◽  
Vol 137 (1) ◽  
pp. 49-54 ◽  
Author(s):  
L G Vallier ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Dna Binding ◽  
Glucose Repression ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Suc2 Promoter ◽  
Repressor Complex ◽  
Glucose Availability

Abstract In the yeast Saccharomyces cerevisiae, glucose repression of SUC2 transcription requires the SSN6-TUP1 repressor complex. It has been proposed that the DNA-binding protein MIG1 secures SSN6-TUP1 to the SUC2 promoter. Here we show that a mig1 deletion does not cause nearly as dramatic a loss of repression as ssn6: glucose-grown mig1 mutants display 20-fold lower SUC2 expression than ssn6 mutants. Thus, repression by SSN6-TUP1 is not mediated solely by MIG1, but also involves MIG1-independent mechanisms. We report that mig1 partially restores SUC2 expression in mutants lacking the SNF1 protein kinase and show that mig1 is allelic to ssn1, a mutation selected as a suppressor of snf1. Other SSN genes identified in this selection were therefore candidates for a role in repression of SUC2. We show that mig1 acts synergistically with ssn2 through ssn5, ssn7, and ssn8 to relieve glucose repression of SUC2 and to suppress the requirement for SNF1. These findings indicate that the SSN proteins contribute to repression of SUC2, and the pleiotropic phenotypes of the ssn mutants suggest global roles in repression. Finally, the regulated SUC2 expression observed in snf1 mig1 mutants indicates that signals regarding glucose availability can be transmitted independently of the SNF1 protein kinase.

scholarly journals An essential Saccharomyces cerevisiae single-stranded DNA binding protein is homologous to the large subunit of human RP-A.

1990 ◽  
Vol 9 (7) ◽  
pp. 2321-2329 ◽  
Author(s):  
W. D. Heyer ◽  
M. R. Rao ◽  
L. F. Erdile ◽  
T. J. Kelly ◽  
R. D. Kolodner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Binding Protein ◽  
Large Subunit ◽  
Dna Binding Protein ◽  
Single Stranded Dna

scholarly journals CC1, a Novel Crenarchaeal DNA Binding Protein

2006 ◽  
Vol 189 (2) ◽  
pp. 403-409 ◽  
Author(s):  
Xiao Luo ◽  
Uli Schwarz-Linek ◽  
Catherine H. Botting ◽  
Reinhard Hensel ◽  
Bettina Siebers ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Nucleic Acid Binding ◽  
Chromatin Protein ◽  
Gene Encoding ◽  
Single Stranded Dna ◽  
Cell Extracts ◽  
Domains Of Life ◽  
High Level

ABSTRACT The genomes of the related crenarchaea Pyrobaculum aerophilum and Thermoproteus tenax lack any obvious gene encoding a single-stranded DNA binding protein (SSB). SSBs are essential for DNA replication, recombination, and repair and are found in all other genomes across the three domains of life. These two archaeal genomes also have only one identifiable gene encoding a chromatin protein (the Alba protein), while most other archaea have at least two different abundant chromatin proteins. We performed a biochemical screen for novel nucleic acid binding proteins present in cell extracts of T. tenax. An assay for proteins capable of binding to a single-stranded DNA oligonucleotide resulted in identification of three proteins. The first protein, Alba, has been shown previously to bind single-stranded DNA as well as duplex DNA. The two other proteins, which we designated CC1 (for crenarchaeal chromatin protein 1), are very closely related to one another, and homologs are restricted to the P. aerophilum and Aeropyrum pernix genomes. CC1 is a 6-kDa, monomeric, basic protein that is expressed at a high level in T. tenax. This protein binds single- and double-stranded DNAs with similar affinities. These properties are consistent with a role for CC1 as a crenarchaeal chromatin protein.

Localization of PURA, the gene encoding the sequence-specific single-stranded-DNA-binding protein Purα, to chromosome band 5q31

1995 ◽  
Vol 71 (1) ◽  
pp. 64-67 ◽  
Author(s):  
Z.-W. Ma ◽  
T. Pejovic ◽  
V. Najfeld ◽  
D.C. Ward ◽  
E.M. Johnson
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Chromosome Band ◽  
Gene Encoding ◽  
Single Stranded Dna
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