Protein-Protein Interactions between the Escherichia coli Single-Stranded DNA-Binding Protein and Exonuclease I

1996 ◽  
Vol 145 (5) ◽  
pp. 619 ◽  
Author(s):  
Margarita Sandigursky ◽  
Frances Mendez ◽  
Robert E. Bases ◽  
Tomohiro Matsumoto ◽  
William A. Franklin
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Exonuclease I

scholarly journals Studies of the Interaction between Rad52 Protein and the Yeast Single-Stranded DNA Binding Protein RPA

1998 ◽  
Vol 18 (7) ◽  
pp. 4400-4406 ◽  
Author(s):  
Sharon L. Hays ◽  
Antoine A. Firmenich ◽  
Philip Massey ◽  
Ronadip Banerjee ◽  
Paul Berg
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Large Subunit ◽  
Critical Role ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Mutant Proteins ◽  
Two Hybrid

ABSTRACT The RFA1 gene encodes the large subunit of the yeast trimeric single-stranded DNA binding protein replication protein A (RPA), which is known to play a critical role in DNA replication. ASaccharomyces cerevisiae strain carrying therfa1-44 allele displays a number of impaired recombination and repair phenotypes, all of which are suppressible by overexpression of RAD52. We demonstrate that a rad52 mutation is epistatic to the rfa1-44 mutation, placingRFA1 and RAD52 in the same genetic pathway. Furthermore, two-hybrid analysis indicates the existence of interactions between Rad52 and all three subunits of RPA. The nature of this Rad52-RPA interaction was further explored by using two different mutant alleles of rad52. Both mutations lie in the amino terminus of Rad52, a region previously defined as being responsible for its DNA binding ability (U. H. Mortenson, C. Beudixen, I. Sunjeuaric, and R. Rothstein, Proc. Natl. Acad. Sci. USA 93:10729–10734, 1996). The yeast two-hybrid system was used to monitor the protein-protein interactions of the mutant Rad52 proteins. Both of the mutant proteins are capable of self-interaction but are unable to interact with Rad51. The mutant proteins also lack the ability to interact with the large subunit of RPA, Rfa1. Interestingly, they retain their ability to interact with the medium-sized subunit, Rfa2. Given the location of the mutations in the DNA binding domain of Rad52, a model incorporating the role of DNA in the protein-protein interactions involved in the repair of DNA double-strand breaks is presented.

scholarly journals F sex factor of Escherichia coli K-12 codes for a single-stranded DNA binding protein.

1983 ◽  
Vol 80 (14) ◽  
pp. 4422-4426 ◽  
Author(s):  
A. L. Kolodkin ◽  
M. A. Capage ◽  
E. I. Golub ◽  
K. B. Low
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
K 12
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