The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase.

The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase.
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DOI:
10.1371/journal.pone.0078141
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Dillingham MS
Dillingham MS
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Gwynn EJ;Smith AJ;Guy CP;Savery NJ;McGlynn P;Dillingham MS

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类UVRD解旋酶在DNA复制、修复和重组途径中发挥着不同的作用。大量新出现的证据表明,它们不同的细胞功能是由与伴侣蛋白的相互作用决定的,这些蛋白将解旋活性靶向适当的底物。最近的研究表明,E.大肠杆菌的研究表明,UvrD可以作为辅助复制解旋酶,解决复制体和转录复合体之间的冲突,但其机制尚不清楚。在这里,我们表明,UVrD同系物PcrA物理相互作用与B。subtilis RNA聚合酶,并且在E.大肠杆菌中,UvrD(而不是密切相关的解旋酶Rep)也与RNA聚合酶相互作用。PcrA-RNAP相互作用是直接的,不依赖于核酸或其他介体蛋白。PcrA的无序但高度保守的C-末端区域,其将PcrA/UvrD与其他相关酶如Rep区分开,对于与RNA聚合酶的相互作用是必要的且充分的。
UvrD-like helicases play diverse roles in DNA replication, repair and recombination pathways. An emerging body of evidence suggests that their different cellular functions are directed by interactions with partner proteins that target unwinding activity to appropriate substrates. Recent studies in E. coli have shown that UvrD can act as an accessory replicative helicase that resolves conflicts between the replisome and transcription complexes, but the mechanism is not understood. Here we show that the UvrD homologue PcrA interacts physically with B. subtilis RNA polymerase, and that an equivalent interaction is conserved in E. coli where UvrD, but not the closely related helicase Rep, also interacts with RNA polymerase. The PcrA-RNAP interaction is direct and independent of nucleic acids or additional mediator proteins. A disordered but highly conserved C-terminal region of PcrA, which distinguishes PcrA/UvrD from otherwise related enzymes such as Rep, is both necessary and sufficient for interaction with RNA polymerase.
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