A Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome

• Published in: Molecular cell Vol. 79; no. 1; pp. 140 - 154.e7
• Main Authors: Monachino, Enrico, Jergic, Slobodan, Lewis, Jacob S., Xu, Zhi-Qiang, Lo, Allen T.Y., O’Shea, Valerie L., Berger, James M., Dixon, Nicholas E., van Oijen, Antoine M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.07.2020
• Subjects: clamp loader-helicase interaction; conformational switch; DNA; DNA Primase - genetics; DNA Primase - metabolism; DNA Replication; DNA, Bacterial; DNA-Directed DNA Polymerase - genetics; DNA-Directed DNA Polymerase - metabolism; DnaB helicase; DnaB Helicases - genetics; DnaB Helicases - metabolism; DnaG primase; enzymes; Escherichia coli - enzymology; Escherichia coli - genetics; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Holoenzymes - chemistry; Holoenzymes - genetics; Holoenzymes - metabolism; Molecular Conformation; polymerase turnover; Protein Binding; Protein Conformation; polymerase turnover; DNA replication; DnaG primase; conformational switch; clamp loader-helicase interaction; DnaB helicase

Recent studies of bacterial DNA replication have led to a picture of the replisome as an entity that freely exchanges DNA polymerases and displays intermittent coupling between the helicase and polymerase(s). Challenging the textbook model of the polymerase holoenzyme acting as a stable complex coor...