Abstract:
:The minichromosome maintenance (MCM) proteins are essential for replication initiation and elongation in eukarya and archaea. There are six MCM proteins in eukaryotes, and MCM complexes are believed to unwind DNA during chromosomal DNA replication. However, the mechanism and structure of the MCM complexes are not known. Only one MCM is found in the archaeon Methanothermobacter thermautotrophicus (mtMCM), and this provides a simpler system for study. The crystal structure of a mtMCM N-terminal fragment has been solved, but surprisingly only subtle structural changes were seen between the wild-type protein and one having a mutation corresponding to the yeast MCM5 bob1 mutation. The bob1 mutation bypasses the phosphorylation required for activation of MCM in yeast. We have used electron microscopy and three-dimensional reconstruction to examine a number of different fragments of mtMCM, and can visualize a large conformational change within the N-terminal fragment. This offers new insight into the conformational dynamics of MCM and the phosphorylation-bypass phenotype in yeast.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Chen YJ,Yu X,Kasiviswanathan R,Shin JH,Kelman Z,Egelman EHdoi
10.1016/j.jmb.2004.11.076keywords:
subject
Has Abstractpub_date
2005-02-18 00:00:00pages
389-94issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(04)01557-8journal_volume
346pub_type
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