A Biochemically Active MCM-like Helicase in Bacillus Cereus

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A Biochemically Active MCM-like Helicase in Bacillus Cereus

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Title: A Biochemically Active MCM-like Helicase in Bacillus Cereus
Author: Samuels, Martin A; Gulati, Gaurav; Shin, Jae-Ho; Opara, Rejoice; McSweeney, Elizabeth; Sekedat, Matt; Long, Stephen; Kelman, Zvi; Jeruzalmi, David

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Citation: Samuels, Martin, Gaurav Gulati, Jae-Ho Shin, Rejoice Opara, Elizabeth McSweeney, Matt Sekedat, Stephen Long, Zvi Kelman, and David Jeruzalmi. 2009. A Biochemically active MCM-like helicase in Bacillus cereus. Nucleic Acids Research 37(13): 4441-52.
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Abstract: The mini-chromosome maintenance (MCM) proteins serve as the replicative helicases in archaea and eukaryotes. Interestingly, an MCM homolog was identified, by BLAST analysis, within a phage integrated in the bacterium Bacillus cereus (Bc). BcMCM is only related to the AAA region of MCM-helicases; the typical amino-terminus is missing and is replaced by a segment with weak homology to primases. We show that BcMCM displays 3'-->5' helicase and ssDNA-stimulated ATPase activity, properties that arise from its conserved AAA domain. Isolated BcMCM is a monomer in solution but likely forms the functional oligomer in vivo. We found that the BcMCM amino-terminus can bind ssDNA and harbors a zinc atom, both hallmarks of the typical MCM amino-terminus. No BcMCM-catalyzed primase activity could be detected. We propose that the divergent amino-terminus of BcMCM is a paralog of the corresponding region of MCM-helicases. A divergent amino terminus makes BcMCM a useful model for typical MCM-helicases since it accomplishes the same function using an apparently unrelated structure.
Published Version: http://dx.doi.org/10.1093/nar/gkp376
Other Sources: http://ukpmc.ac.uk/articlerender.cgi?tool=pubmed&pubmedid=19474351
Terms of Use: This article is made available under the terms and conditions applicable to Open Access Policy Articles, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#OAP
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:3355780

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  • FAS Scholarly Articles [7106]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
 
 

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