Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes.
Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes.
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DOI:
10.1093/nar/gkq161
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发表时间:
2010-07
影响因子:
14.9
通讯作者:
Xu W
中科院分区:
文献类型:
--
作者:
Schumacher MA;Piro KM;Xu W
Accurate DNA segregation is essential for genome transmission. Segregation of the prototypical F plasmid requires the centromere-binding protein SopB, the NTPase SopA and the sopC centromere. SopB displays an intriguing range of DNA-binding properties essential for partition; it binds sopC to form a partition complex, which recruits SopA, and it also coats DNA to prevent non-specific SopA–DNA interactions, which inhibits SopA polymerization. To understand the myriad functions of SopB, we determined a series of SopB–DNA crystal structures. SopB does not distort its DNA site and our data suggest that SopB–sopC forms an extended rather than wrapped partition complex with the SopA-interacting domains aligned on one face. SopB is a multidomain protein, which like P1 ParB contains an all-helical DNA-binding domain that is flexibly attached to a compact (β3–α)2 dimer-domain. Unlike P1 ParB, the SopB dimer-domain does not bind DNA. Moreover, SopB contains a unique secondary dimerization motif that bridges between DNA duplexes. Both specific and non-specific SopB–DNA bridging structures were observed. This DNA-linking function suggests a novel mechanism for in trans DNA spreading by SopB, explaining how it might mask DNA to prevent DNA-mediated inhibition of SopA polymerization.
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DOI:
10.1073/pnas.0507222102
发表时间:
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影响因子:
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