scholarly journals The role of the 6 lysines and the terminal amine ofescherichia colisingle-strand binding protein in its binding of single-stranded DNA

1998 ◽  
Vol 7 (8) ◽  
pp. 1781-1788 ◽  
Author(s):  
Jiwen Chen ◽  
David L. Smith ◽  
Mark A. Griep
Blood ◽  
2007 ◽  
Vol 110 (7) ◽  
pp. 2390-2398 ◽  
Author(s):  
Rigu Gupta ◽  
Sudha Sharma ◽  
Joshua A. Sommers ◽  
Mark K. Kenny ◽  
Sharon B. Cantor ◽  
...  

The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability.


PLoS Genetics ◽  
2011 ◽  
Vol 7 (6) ◽  
pp. e1002156 ◽  
Author(s):  
Laetitia Attaiech ◽  
Audrey Olivier ◽  
Isabelle Mortier-Barrière ◽  
Anne-Lise Soulet ◽  
Chantal Granadel ◽  
...  

1980 ◽  
Vol 210 (1180) ◽  
pp. 337-349 ◽  

The gene A protein of bacteriophage ɸX 174 initiates replication of super-twisted RFI DNA by cleaving the viral (+) strand at the origin of replication and binding to the 5' end. Upon addition of E. coli rep protein (single-stranded DNA dependent ATPase), E. coli single-stranded DNA binding protein and ATP, complete unwinding of the two strands occurs. Electron microscopic analyses of intermediates in the reaction reveal that the unwinding occurs by movement of the 5' end into the duplex, displacing the viral strand in the form of a single-stranded loop. Since unwinding will not occur in the absence of either gene A protein or rep protein, it is presumed that the rep protein interacts to form a complex with the bound gene A protein. Single-stranded DNA binding protein facilitates the unwinding by binding to the exposed single-stranded DNA. Further addition of the four deoxyribotriphosphates and DNA polymerase III holoenzyme to the reaction results in synthesis of viral (+) single-stranded circles in amounts exceeding that of the input template. A model describing the role of gene A protein and rep protein in duplex DNA replication is presented and other properties of gene A protein discussed.


2018 ◽  
Vol 30 (6) ◽  
pp. 761
Author(s):  
Mi-Ra Choi ◽  
Jung-Min Shin ◽  
Young-Ah Shin ◽  
Yun-Hee Chang ◽  
Min-Youl Chang ◽  
...  

FEBS Letters ◽  
1987 ◽  
Vol 211 (2) ◽  
pp. 155-159 ◽  
Author(s):  
Mustafa I. Khamis ◽  
Jose R. Casas-Finet ◽  
August H. Maki ◽  
Janet B. Murphy ◽  
John W. Chase

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