Journal
MOLECULAR CELL
Volume 28, Issue 2, Pages 304-314Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.08.013
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Funding
- Medical Research Council [MC_U105370180] Funding Source: Medline
- Medical Research Council [MC_U105370180] Funding Source: researchfish
- MRC [MC_U105370180] Funding Source: UKRI
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The subunits of the presumptive replicative helicase of archaea and eukaryotes, the MCM complex, are members of the AAA+ (ATPase-associated with various cellular activities) family of ATPases. Proteins within this family harness the chemical energy of ATP hydrolysis to perform a broad range of cellular processes. Here, we investigate the function of the AAA+ site in the mini-chromosome maintenance (MCM) complex of the archaeon Sulfolobus solfataricus (SsoMCM). We find that SsoMCM has an unusual active-site architecture, with a unique blend of features previously found only in distinct families of AAA+ proteins. We additionally describe a series of mutant doping experiments to investigate the mechanistic basis of inter-subunit coordination in the generation of helicase activity. Our results indicate that MCM can tolerate catalytically inactive subunits and still function as a helicase, leading us to propose a semisequential model for helicase activity of this complex.
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