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A novel zinc finger is required for Mcm10 homocomplex assembly. J Biol Chem 2003 Sep 19;278(38):36051-8

Date

07/08/2003

Pubmed ID

12844493

DOI

10.1074/jbc.M306049200

Scopus ID

2-s2.0-0141815735   30 Citations

Abstract

Mcm10 is a DNA replication factor that interacts with multiple subunits of the MCM2-7 hexameric complex. We report here that Mcm10 self-interacts and assembles into large homocomplexes (approximately 800 kDa). A conserved domain of 210 amino acid residues is sufficient for mediating self-interaction and complex assembly. A novel zinc finger within the conserved domain, CX10CX11CX2H, is essential for the homocomplex formation. Mutant alleles with amino acid substitutions at conserved cysteines and histidine in the zinc finger fail to assemble homocomplexes. A defect in homocomplex assembly correlates with defects in DNA replication and cell growth in the mutants. These observations suggest that homocomplex assembly is essential for Mcm10 function. Multisubunit Mcm10 homocomplexes may provide the structural basis for Mcm10 to interact with multiple subunits of the MCM2-7 hexamer.

Author List

Cook CR, Kung G, Peterson FC, Volkman BF, Lei M

Authors

Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Alleles
Amino Acid Motifs
Amino Acids
Blotting, Western
Cell Cycle Proteins
Cell Division
Chromatography, Gel
Chromosomal Proteins, Non-Histone
Cysteine
DNA
Fungal Proteins
Genetic Vectors
Glutathione Transferase
Histidine
Magnetic Resonance Spectroscopy
Minichromosome Maintenance Proteins
Peptides
Phenotype
Plasmids
Protein Binding
Protein Structure, Tertiary
Recombinant Fusion Proteins
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Zinc
Zinc Fingers
beta-Galactosidase
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46