Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 13, Pages 11855-11864Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.199521
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Funding
- CRUK [C303/A3135, C303/A8102, C303/A7399, C303/A5434]
- BBSRC [BB/H013024/1]
- Wellcome Trust [08136/Z/06/Z, 083524/Z/07/Z]
- BBSRC [BB/H013024/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H013024/1] Funding Source: researchfish
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In late mitosis and G1, Mcm2-7 are assembled onto replication origins to license them for initiation in the upcoming S phase. After initiation, Mcm2-7 provide helicase activity to unwind DNA at the replication fork. Here we examine the structure of Mcm2-7 on chromatin in Xenopus egg extracts. We show that prior to replication initiation, Mcm2-7 is present at licensed replication origins in a complex with a molecular mass close to double that of the Mcm2-7 hexamer. This complex has approximately stoichiometric quantities of the 6 Mcm2-7 proteins and we conclude that it consists of a double heterohexamer. This provides a configuration potentially capable of initiating a pair of bidirectional replication forks in S phase. We also show that after initiation, Mcm2-7 associate with Cdc45 and GINS to form a relatively stable CMG (Cdc45-MCM-GINS) complex. The CMG proteins also associate less strongly with other replication proteins, consistent with the idea that a single CMG complex forms the core of the replisome.
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