scholarly journals Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme

1991 ◽  
Vol 266 (17) ◽  
pp. 11328-11334 ◽  
Author(s):  
P.T. Stukenberg ◽  
P.S. Studwell-Vaughan ◽  
M. O'Donnell
2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Andrea Bogutzki ◽  
Natalie Naue ◽  
Lidia Litz ◽  
Andreas Pich ◽  
Ute Curth

Abstract During DNA replication in E. coli, a switch between DnaG primase and DNA polymerase III holoenzyme (pol III) activities has to occur every time when the synthesis of a new Okazaki fragment starts. As both primase and the χ subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB), it had been proposed that the binding of both proteins to SSB is mutually exclusive. Using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB, we tested whether DnaG and pol III can bind concurrently to the primed template. We found that the addition of pol III does not lead to a displacement of primase, but to the formation of higher complexes. Even pol III-mediated primer elongation by one or several DNA nucleotides does not result in the dissociation of DnaG. About 10 nucleotides have to be added in order to displace one of the two primase molecules bound to SSB-saturated G4ori. The concurrent binding of primase and pol III is highly plausible, since even the SSB tetramer situated directly next to the 3′-terminus of the primer provides four C-termini for protein-protein interactions.


1984 ◽  
Vol 259 (9) ◽  
pp. 5567-5573
Author(s):  
R DiFrancesco ◽  
S K Bhatnagar ◽  
A Brown ◽  
M J Bessman

Sign in / Sign up

Export Citation Format

Share Document