scholarly journals Water skating: How polymerase sliding clamps move on DNA

FEBS Journal ◽  
2021 ◽  
Author(s):  
Huilin Li ◽  
Fengwei Zheng ◽  
Mike O’Donnell
Keyword(s):  



Author(s):  
Amanda S. Altieri ◽  
Zvi Kelman


PLoS ONE ◽  
2016 ◽  
Vol 11 (5) ◽  
pp. e0154899 ◽  
Author(s):  
Aaron J. Oakley
Keyword(s):  


Nature ◽  
2016 ◽  
Vol 539 (7630) ◽  
pp. 583-587 ◽  
Author(s):  
Jiaquan Liu ◽  
Jeungphill Hanne ◽  
Brooke M. Britton ◽  
Jared Bennett ◽  
Daehyung Kim ◽  
...  


2000 ◽  
Vol 10 (1) ◽  
pp. R25-R29 ◽  
Author(s):  
Manju M. Hingorani ◽  
Mike O’Donnell
Keyword(s):  




eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Mark Hedglin ◽  
Senthil K Perumal ◽  
Zhenxin Hu ◽  
Stephen Benkovic

In most organisms, clamp loaders catalyze both the loading of sliding clamps onto DNA and their removal. How these opposing activities are regulated during assembly of the DNA polymerase holoenzyme remains unknown. By utilizing FRET to monitor protein-DNA interactions, we examined assembly of the human holoenzyme. The results indicate that assembly proceeds in a stepwise manner. The clamp loader (RFC) loads a sliding clamp (PCNA) onto a primer/template junction but remains transiently bound to the DNA. Unable to slide away, PCNA re-engages with RFC and is unloaded. In the presence of polymerase (polδ), loaded PCNA is captured from DNA-bound RFC which subsequently dissociates, leaving behind the holoenzyme. These studies suggest that the unloading activity of RFC maximizes the utilization of PCNA by inhibiting the build-up of free PCNA on DNA in the absence of polymerase and recycling limited PCNA to keep up with ongoing replication.



2021 ◽  
Vol 120 (1) ◽  
pp. 73-85
Author(s):  
Anirban Purohit ◽  
Lauren G. Douma ◽  
Linda B. Bloom ◽  
Marcia Levitus


2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Jiaquan Liu ◽  
Ryanggeun Lee ◽  
Brooke M. Britton ◽  
James A. London ◽  
Keunsang Yang ◽  
...  

AbstractA shared paradigm of mismatch repair (MMR) across biology depicts extensive exonuclease-driven strand-specific excision that begins at a distant single-stranded DNA (ssDNA) break and proceeds back past the mismatched nucleotides. Historical reconstitution studies concluded that Escherichia coli (Ec) MMR employed EcMutS, EcMutL, EcMutH, EcUvrD, EcSSB and one of four ssDNA exonucleases to accomplish excision. Recent single-molecule images demonstrated that EcMutS and EcMutL formed cascading sliding clamps on a mismatched DNA that together assisted EcMutH in introducing ssDNA breaks at distant newly replicated GATC sites. Here we visualize the complete strand-specific excision process and find that long-lived EcMutL sliding clamps capture EcUvrD helicase near the ssDNA break, significantly increasing its unwinding processivity. EcSSB modulates the EcMutL–EcUvrD unwinding dynamics, which is rarely accompanied by extensive ssDNA exonuclease digestion. Together these observations are consistent with an exonuclease-independent MMR strand excision mechanism that relies on EcMutL–EcUvrD helicase-driven displacement of ssDNA segments between adjacent EcMutH–GATC incisions.



Author(s):  
D.S. Goodsell
Keyword(s):  


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