scholarly journals Using Site Specific Fluorescent Probes to Examine Replication Fork Destabilization by Regulatory Proteins of the Bacteriophage T4 DNA Replication Complex

2017 ◽  
Vol 112 (3) ◽  
pp. 314a-315a
Author(s):  
Davis Jose ◽  
Miya Mary Michael ◽  
Wonbae Lee ◽  
Thomas H. Steinberg ◽  
Andrew H. Marcus ◽  
...  
2004 ◽  
Vol 279 (18) ◽  
pp. 19035-19045 ◽  
Author(s):  
Yujie Ma ◽  
Tongsheng Wang ◽  
Jana L. Villemain ◽  
David P. Giedroc ◽  
Scott W. Morrical

1996 ◽  
Vol 271 (45) ◽  
pp. 28045-28051 ◽  
Author(s):  
Daniel J. Sexton ◽  
Theodore E. Carver ◽  
Anthony J. Berdis ◽  
Stephen J. Benkovic

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Nicolai B. Larsen ◽  
Ehud Sass ◽  
Catherine Suski ◽  
Hocine W. Mankouri ◽  
Ian D. Hickson

2003 ◽  
Vol 278 (28) ◽  
pp. 25435-25447 ◽  
Author(s):  
Emmanuelle Delagoutte ◽  
Peter H. von Hippel

2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Maria Manosas ◽  
Senthil K. Perumal ◽  
Piero R. Bianco ◽  
Felix Ritort ◽  
Stephen J. Benkovic ◽  
...  

Abstract Helicases that both unwind and rewind DNA have central roles in DNA repair and genetic recombination. In contrast to unwinding, DNA rewinding by helicases has proved difficult to characterize biochemically because of its thermodynamically downhill nature. Here we use single-molecule assays to mechanically destabilize a DNA molecule and follow, in real time, unwinding and rewinding by two DNA repair helicases, bacteriophage T4 UvsW and Escherichia coli RecG. We find that both enzymes are robust rewinding enzymes, which can work against opposing forces as large as 35 pN, revealing their active character. The generation of work during the rewinding reaction allows them to couple rewinding to DNA unwinding and/or protein displacement reactions central to the rescue of stalled DNA replication forks. The overall results support a general mechanism for monomeric rewinding enzymes.


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