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Publication Detail
ATPase site architecture and helicase mechanism of an archaeal MCM
  • Publication Type:
    Journal article
  • Publication Sub Type:
    JOUR
  • Authors:
    Moreau MJ, McGeoch AT, Lowe AR, Itzhaki LS, Bell SD
  • Publication date:
    2007
  • Pagination:
    304, 314
  • Journal:
    Mol Cell
  • Volume:
    28
  • Medium:
    2
  • Print ISSN:
    1097-2765
  • Keywords:
    Adenosine Triphosphate/ metabolism Archaeal Proteins/ chemistry/genetics/metabolism Binding Sites Computer Simulation DNA Helicases/ chemistry/genetics/metabolism Hydrolysis Metalloendopeptidases/chemistry/genetics/ metabolism Models, Chemical Models, Molecular Monte Carlo Method Multiprotein Complexes/chemistry Mutagenesis, Site-Directed Protein Conformation Protein Subunits Sulfolobus solfataricus/ enzymology/genetics
  • Notes:
    Moreau, Matthew J McGeoch, Adam T Lowe, Alan R Itzhaki, Laura S Bell, Stephen D Research Support, Non-U.S. Gov't Molecular cell S1097-2765(07)00556-4 [pii] Mol Cell. 2007 Oct 26;28(2):304-14. 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 intersubunit 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.
Abstract
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 intersubunit 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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