ParB Partition Proteins: Complex Formation and Spreading at Bacterial and Plasmid Centromeres.

ParB Partition Proteins: Complex Formation and Spreading at Bacterial and Plasmid Centromeres.
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DOI:
10.3389/fmolb.2016.00044
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发表时间:
2016
影响因子:
5
通讯作者:
Funnell BE
Funnell BE
中科院分区:
生物学3区
文献类型:
--
作者:
Funnell BE

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在细菌中,主动分配系统有助于染色体和低拷贝数质粒的忠实分离。每个系统都依赖于一个位点特异性DNA结合蛋白来识别和组装一个位于着丝粒样位点的分区复合物,通常称为parS。许多质粒和所有染色体着丝粒结合蛋白都是二聚体螺旋-转角-螺旋DNA结合蛋白,通常称为ParB。虽然ParB之间的整体序列保守性不高,但蛋白质共享相似的结构域和功能组织,并且它们组装成相似的高阶复合物。在体内,ParB“扩散”,也就是说,DNA结合从parS位点延伸到周围的非特异性DNA中,这一特征反映了更高阶的复杂组装。ParB在parS和非特异性DNA位点桥接和配对DNA。ParB二聚体通过N-末端区域的灵活构象彼此相互作用。这篇评论将集中在HTH着丝粒结合蛋白的性质,在最近的实验证据和模型,增加了我们的理解,这些蛋白质如何组装成大型和动态的分区复合物在其特定的DNA位点和周围。
In bacteria, active partition systems contribute to the faithful segregation of both chromosomes and low-copy-number plasmids. Each system depends on a site-specific DNA binding protein to recognize and assemble a partition complex at a centromere-like site, commonly called parS. Many plasmid, and all chromosomal centromere-binding proteins are dimeric helix-turn-helix DNA binding proteins, which are commonly named ParB. Although the overall sequence conservation among ParBs is not high, the proteins share similar domain and functional organization, and they assemble into similar higher-order complexes. In vivo, ParBs “spread,” that is, DNA binding extends away from the parS site into the surrounding non-specific DNA, a feature that reflects higher-order complex assembly. ParBs bridge and pair DNA at parS and non-specific DNA sites. ParB dimers interact with each other via flexible conformations of an N-terminal region. This review will focus on the properties of the HTH centromere-binding protein, in light of recent experimental evidence and models that are adding to our understanding of how these proteins assemble into large and dynamic partition complexes at and around their specific DNA sites.
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