Abstract
The minichromosome maintenance (MCM) complex is thought to function as the replicative helicase in archaea and eukarya. The structure of the single MCM protein homologue from the archaeon Methanothermobacter thermautotrophicus is not yet clear, and hexameric, heptameric, octameric, and dodecameric structures, open rings, and filamentous structures have been reported. Using a combination of biochemical and structural analysis, it is shown here that the M. thermautotrophicus MCM helicase is active as a hexamer.
Highlights
The structure of the archaeal minichromosome maintenance (MCM) complex is unclear
The Methanothermobacter thermautotrophicus enzyme is the only exception, as it appears to form dodecamers [12,13,14], and a dodecameric structure was suggested by the crystal structure of the N-terminal portion of the protein [15] and an electron microscopic analysis of the full-length enzyme (16 –18)
These studies suggested that hexamers are the active form of the M. thermautotrophicus MCM helicase
Summary
Labeled and unlabeled nucleotides were purchased from GE Healthcare. Oligonucleotides were synthesized by the DNA facility at the Center for Advanced Research in Biotechnology. The MCM protein containing a cAMP-dependent protein kinase recognition motif was purified as described previously [22]
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