Open AccessHigh‐Molecular‐Mass Complexes of Human Minichromosome‐Maintenance Proteins in Mitotic Cells
Author(s) -
Richter Andreas,
Knippers Rolf
Publication year - 1997
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1997.00136.x
Subject(s) - minichromosome maintenance , multiprotein complex , minichromosome , chromatin , mitosis , microbiology and biotechnology , nucleoplasm , biology , origin recognition complex , interphase , dna replication , eukaryotic dna replication , dna , genetics , nucleus , gene , nucleolus
Minichromosome‐maintenance (Mcm) proteins perform essential functions regulating the replication of eukaryotic genomes. In interphase cells they are either bound to a nuclear structure, most probably chromatin, or occur as free multiprotein complexes in the nucleoplasm. Mcm proteins are displaced from their chromatin sites during S phase, and several become highly phosphorylated during mitosis. We investigated whether phosphorylation affects the ability of mitotic Mcm proteins to form multiprotein complexes. Our results clearly show that phosphorylated mitotic Mcm proteins form a 14–15‐S complex, probably consisting of one molecule each of the six known human Mcm proteins.