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质粒P1的ParA分区蛋白发生改变后,通过分区位点发挥作用,阻止质粒的复制。

Altered ParA partition proteins of plasmid P1 act via the partition site to block plasmid propagation.

作者信息

Youngren B, Austin S

机构信息

ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702-1201, USA.

出版信息

Mol Microbiol. 1997 Sep;25(6):1023-30. doi: 10.1046/j.1365-2958.1997.4761842.x.

Abstract

The partition system of the P1 plasmid, P1par, consists of the ParA and ParB proteins and a cis-acting site, parS. It is responsible for the orderly segregation of plasmid copies to daughter cells. Plasmids with null mutations in parA or parB replicate normally, but missegregate. ParB binds specifically to the parS site, but the role of ParA and its ATPase activity in partition is unclear. We describe a novel class of parA mutants that cannot be established or maintained as plasmids unless complemented by the wild-type gene. One, parAM314l, is conditional: it can be maintained in cells in minimal medium but cannot be established in cells growing in L broth. The lack of plasmid propagation in L broth-grown cells was shown to be caused by a ParB-dependent activity of the mutant ParA protein that blocks plasmid propagation by an interaction at the parS site. Thus, ParA acts to modify the ParB-parS complex, probably by binding to it. Partition is thought to involve selection of pairs of plasmids before segregation, either by physical pairing of copies or by binding of copies to paired host sites. We suggest that ParA is involved in this reaction and that the mutant ParA protein forms paired complexes that cannot unpair.

摘要

P1 质粒的分配系统 P1par 由 ParA 和 ParB 蛋白以及一个顺式作用位点 parS 组成。它负责将质粒拷贝有序地分配到子细胞中。在 parA 或 parB 中具有无效突变的质粒能够正常复制,但会发生错配。ParB 特异性地结合 parS 位点,但 ParA 及其 ATP 酶活性在分配过程中的作用尚不清楚。我们描述了一类新型的 parA 突变体,除非由野生型基因互补,否则它们不能作为质粒被建立或维持。其中一个突变体 parAM314l 具有条件性:它可以在基本培养基中的细胞中维持,但不能在 L 肉汤中生长的细胞中建立。在 L 肉汤中生长的细胞中缺乏质粒增殖被证明是由突变型 ParA 蛋白的一种依赖于 ParB 的活性引起的,这种活性通过在 parS 位点的相互作用来阻断质粒增殖。因此,ParA 可能通过与 ParB-parS 复合物结合来对其进行修饰。分配过程被认为在分离之前涉及对质粒对的选择,这要么通过拷贝的物理配对,要么通过拷贝与配对的宿主位点的结合来实现。我们认为 ParA 参与了这个反应,并且突变型 ParA 蛋白形成了无法解开的配对复合物。

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