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      Quality control in the initiation of eukaryotic DNA replication

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          Abstract

          Origins of DNA replication must be regulated to ensure that the entire genome is replicated precisely once in each cell cycle. In human cells, this requires that tens of thousands of replication origins are activated exactly once per cell cycle. Failure to do so can lead to cell death or genome rearrangements such as those associated with cancer. Systems ensuring efficient initiation of replication, while also providing a robust block to re-initiation, play a crucial role in genome stability. In this review, I will discuss some of the strategies used by cells to ensure once per cell cycle replication and provide a quantitative framework to evaluate the relative importance and efficiency of individual pathways involved in this regulation.

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          Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing.

          Dirk Remus, Fabienne Beuron, Gökhan Tolun … (2009)
          The licensing of eukaryotic DNA replication origins, which ensures once-per-cell-cycle replication, involves the loading of six related minichromosome maintenance proteins (Mcm2-7) into prereplicative complexes (pre-RCs). Mcm2-7 forms the core of the replicative DNA helicase, which is inactive in the pre-RC. The loading of Mcm2-7 onto DNA requires the origin recognition complex (ORC), Cdc6, and Cdt1, and depends on ATP. We have reconstituted Mcm2-7 loading with purified budding yeast proteins. Using biochemical approaches and electron microscopy, we show that single heptamers of Cdt1*Mcm2-7 are loaded cooperatively and result in association of stable, head-to-head Mcm2-7 double hexamers connected via their N-terminal rings. DNA runs through a central channel in the double hexamer, and, once loaded, Mcm2-7 can slide passively along double-stranded DNA. Our work has significant implications for understanding how eukaryotic DNA replication origins are chosen and licensed, how replisomes assemble during initiation, and how unwinding occurs during DNA replication.
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            GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks.

            Agnieszka Gambus, Richard Jones, Alberto Sanchez-Diaz … (2006)
            The components of the replisome that preserve genomic stability by controlling the progression of eukaryotic DNA replication forks are poorly understood. Here, we show that the GINS (go ichi ni san) complex allows the MCM (minichromosome maintenance) helicase to interact with key regulatory proteins in large replisome progression complexes (RPCs) that are assembled during initiation and disassembled at the end of S phase. RPC components include the essential initiation and elongation factor, Cdc45, the checkpoint mediator Mrc1, the Tof1-Csm3 complex that allows replication forks to pause at protein-DNA barriers, the histone chaperone FACT (facilitates chromatin transcription) and Ctf4, which helps to establish sister chromatid cohesion. RPCs also interact with Mcm10 and topoisomerase I. During initiation, GINS is essential for a specific subset of RPC proteins to interact with MCM. GINS is also important for the normal progression of DNA replication forks, and we show that it is required after initiation to maintain the association between MCM and Cdc45 within RPCs.
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              Evolutionary relationships and structural mechanisms of AAA+ proteins.

              Jan Erzberger, James M Berger (2006)
              Complex cellular events commonly depend on the activity of molecular "machines" that efficiently couple enzymatic and regulatory functions within a multiprotein assembly. An essential and expanding subset of these assemblies comprises proteins of the ATPases associated with diverse cellular activities (AAA+) family. The defining feature of AAA+ proteins is a structurally conserved ATP-binding module that oligomerizes into active arrays. ATP binding and hydrolysis events at the interface of neighboring subunits drive conformational changes within the AAA+ assembly that direct translocation or remodeling of target substrates. In this review, we describe the critical features of the AAA+ domain, summarize our current knowledge of how this versatile element is incorporated into larger assemblies, and discuss specific adaptations of the AAA+ fold that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Philos Trans R Soc Lond B Biol Sci
                Journal ID (publisher-id): RSTB
                Journal ID (hwp): royptb
                Title: Philosophical Transactions of the Royal Society B: Biological Sciences
                Publisher: The Royal Society
                ISSN (Print): 0962-8436
                ISSN (Electronic): 1471-2970
                Publication date (Print): 27 December 2011
                Publication date PMC-release: 27 December 2011
                Volume: 366
                Issue: 1584 , Theme Issue 'The cell cycle' compiled and edited by Béla Novák, Tim Hunt and Kim Nasmyth
                Pages: 3545-3553
                Affiliations
                Cancer Research UK London Research Institute, simpleClare Hall Laboratories , South Mimms, Herts EN6 3LD, UK
                Author notes

                One contribution of 16 to a Theme Issue ‘ The cell cycle’.

                Article
                Publisher ID: rstb20110073
                DOI: 10.1098/rstb.2011.0073
                PMC ID: 3203456
                PubMed ID: 22084381
                SO-VID: ad4951a9-829a-4deb-9af7-99b1ed01699e
                Copyright © This journal is © 2011 The Royal Society
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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                Subject: 1001
                Subject: 15
                Subject: Articles
                Subject: Review Article

                ScienceOpen disciplines: Philosophy of science
                Keywords: cell cycle,dna replication,s phase
                Data availability:
                ScienceOpen disciplines: Philosophy of science
                Keywords: cell cycle, dna replication, s phase

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