由聚合蛋白ParF介导的细菌DNA分离动力学
Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF.
作者信息
Barillà Daniela, Rosenberg Mark F, Nobbmann Ulf, Hayes Finbarr
机构信息
Faculty of Life Sciences, University of Manchester, Manchester, UK.
出版信息
EMBO J. 2005 Apr 6;24(7):1453-64. doi: 10.1038/sj.emboj.7600619. Epub 2005 Mar 10.
Abstract
Prokaryotic DNA segregation most commonly involves members of the Walker-type ParA superfamily. Here we show that the ParF partition protein specified by the TP228 plasmid is a ParA ATPase that assembles into extensive filaments in vitro. Polymerization is potentiated by ATP binding and does not require nucleotide hydrolysis. Analysis of mutations in conserved residues of the Walker A motif established a functional coupling between filament dynamics and DNA partitioning. The partner partition protein ParG plays two separable roles in the ParF polymerization process. ParF is unrelated to prokaryotic polymerizing proteins of the actin or tubulin families, but is a homologue of the MinD cell division protein, which also assembles into filaments. The ultrastructures of the ParF and MinD polymers are remarkably similar. This points to an evolutionary parallel between DNA segregation and cytokinesis in prokaryotic cells, and reveals a potential molecular mechanism for plasmid and chromosome segregation mediated by the ubiquitous ParA-type proteins.
摘要
原核生物的DNA分离通常涉及沃克型ParA超家族的成员。我们在此表明，由TP228质粒指定的ParF分配蛋白是一种ParA ATP酶，它在体外组装成广泛的细丝。ATP结合增强了聚合作用，且不需要核苷酸水解。对沃克A基序保守残基突变的分析确定了细丝动力学与DNA分配之间的功能耦合。伙伴分配蛋白ParG在ParF聚合过程中发挥两个可分离的作用。ParF与肌动蛋白或微管蛋白家族的原核聚合蛋白无关，但与MinD细胞分裂蛋白同源，后者也组装成细丝。ParF和MinD聚合物的超微结构非常相似。这表明原核细胞中DNA分离和胞质分裂之间存在进化上的平行关系，并揭示了由普遍存在的ParA型蛋白介导的质粒和染色体分离的潜在分子机制。
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