Author:
Indiani Chiara,O'Donnell Mike
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Reference127 articles.
1. Johnson, A. & O'Donnell, M. Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem. 74, 283–315 (2005).
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4. Miyata, T. et al. Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. Proc. Natl Acad. Sci. USA 102, 13795–13800 (2005). The EM structure of an archaeal RFC–PCNA–DNA complex in the presence of ATPγS shows the clamp in an open state. The open PCNA has a lock-washer conformation and fits onto the AAA+ surface of RFC. Density that probably corresponds to DNA is observed in the centre of PCNA and in the central chamber of RFC. The complex might represent an intermediate in which PCNA is kept open before ATP hydrolysis by RFC.
5. Bowman, G. D., O'Donnell, M. & Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex. Nature 429, 724–730 (2004). The S. cerevisiae RFC–PCNA–ATPγS structure indicates a mechanism for DNA engagement by the AAA+ clamp-loader assembly. The ATPase domains of RFC are arranged in a right-handed spiral that complements the structure of dsDNA modelled inside. The PCNA lies below the RFC spiral in a closed conformation, which indicates that ring closure might precede hydrolysis of ATP.
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