A biochemically active MCM-like helicase in Bacillus cereus.
A biochemically active MCM-like helicase in Bacillus cereus.
复制标题
蜡样芽孢杆菌中具有生化活性的 MCM 样解旋酶。
DOI：
10.1093/nar/gkp376
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发表时间：
2009
影响因子：
14.9
通讯作者：
Jeruzalmi,David
中科院分区：
文献类型：
--
作者：
Samuels,Martin;Gulati,Gaurav;Shin,Jae-Ho;Opara,Rejoice;McSweeney,Elizabeth;Sekedat,Matt;Long,Stephen;Kelman,Zvi;Jeruzalmi,David
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 bacteriumBacillus 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 thatBcMCM displays 3′→5′ helicase and ssDNA-stimulated ATPase activity, properties that arise from its conserved AAA domain. IsolatedBcMCM is a monomer in solution but likely forms the functional oligomerin vivo. We found that theBcMCM amino-terminus can bind ssDNA and harbors a zinc atom, both hallmarks of the typical MCM amino-terminus. NoBcMCM-catalyzed primase activity could be detected. We propose that the divergent amino-terminus ofBcMCM is a paralog of the corresponding region of MCM-helicases. A divergent amino terminus makesBcMCM a useful model for typical MCM-helicases since it accomplishes the same function using an apparently unrelated structure.
