Cannone, G., Xu, Y., Beattie, T. R., Bell, S. D. and Spagnolo, L. (2015) The architecture of an Okazaki fragment-processing holoenzyme from the archaeon Sulfolobus solfataricus. Biochemical Journal, 465(2), pp. 239-245. (doi: 10.1042/BJ20141120) (PMID:25299633)
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Abstract
DNA replication on the lagging strand occurs via the synthesis and maturation of Okazaki fragments. In archaea and eukaryotes, the enzymatic activities required for this process are supplied by a replicative DNA polymerase, Flap endonuclease 1 (Fen1) and DNA ligase 1 (Lig1). These factors interact with the sliding clamp PCNA (proliferating cell nuclear antigen) providing a potential means of co-ordinating their sequential actions within a higher order assembly. In hyperthermophilic archaea of the Sulfolobus genus, PCNA is a defined heterotrimeric assembly and each subunit interacts preferentially with specific client proteins. We have exploited this inherent asymmetry to assemble a PCNA-polymerase-Fen1-ligase complex on DNA and have visualized it by electron microscopy. Our studies reveal the structural basis of co-occupancy of a single PCNA ring by the three distinct client proteins.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Spagnolo, Professor Laura |
Authors: | Cannone, G., Xu, Y., Beattie, T. R., Bell, S. D., and Spagnolo, L. |
College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
Journal Name: | Biochemical Journal |
Publisher: | Portland Press |
ISSN: | 0264-6021 |
ISSN (Online): | 1470-8728 |
Published Online: | 09 October 2014 |
Copyright Holders: | Copyright © 2014 The Authors |
First Published: | First published in Biochemical Journal 465(2):239-245 |
Publisher Policy: | Reproduced under a Creative Commons License |
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