Hold on!: RNA polymerase interactions with the nascent RNA modulate transcription elongation and termination.

Hold on!: RNA polymerase interactions with the nascent RNA modulate transcription elongation and termination.
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DOI:
10.4161/rna.7.3.11912
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发表时间:
2010-05
期刊:
影响因子:
4.1
通讯作者:
Werner F
Werner F
中科院分区:
生物学3区
文献类型:
--
作者:
Grohmann D;Werner F

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来自真核生物、古细菌和细菌这三个生命领域的进化相关的多亚单位RNA聚合酶具有共同的结构和功能特性。我们最近发现,两个RNAP亚基F/E(RPB4/7)-在真核细胞和古生菌之间保守,但没有细菌同源物-与新生的RNA链相互作用,从而深刻地调节RNAP活性。总体而言,F/E增加了转录的加工性,但它也以一种依赖于序列的方式刺激转录终止。除了RNA结合,这两个明显相反的过程可能涉及RNAP钳的变构机制。Spt4/5是唯一已知的在生命的所有三个结构域都保守的RNAP相关转录因子,它刺激类似于RNAP亚基F/E的伸长,Spt4/5通过与RNAP钳相互作用,以一种独立于非模板DNA链的方式增强加工性。虽然Spt4/5的分子机制在进化中是普遍保守的,但在细菌和古真核生物谱系分裂后,F/E类复合体的附加功能已经出现。有趣的是,理论上,噬菌体编码的抗终止子蛋白可以在细菌RNAP中发挥类似的功能。
Evolutionary related multisubunit RNA polymerases from all three domains of life, Eukarya, Archaea and Bacteria, have common structural and functional properties. We have recently shown that two RNAP subunits, F/E (RPB4/7)—which are conserved between eukaryotes and Archaea but have no bacterial homologues—interact with the nascent RNA chain and thereby profoundly modulate RNAP activity. Overall F/E increases transcription processivity, but it also stimulates transcription termination in a sequence-dependent manner. In addition to RNA-binding, these two apparently opposed processes are likely to involve an allosteric mechanism of the RNAP clamp. Spt4/5 is the only known RNAP-associated transcription factor that is conserved in all three domains of life, and it stimulates elongation similar to RNAP subunits F/E. Spt4/5 enhances processivity in a fashion that is independent of the nontemplate DNA strand, by interacting with the RNAP clamp. Whereas the molecular mechanism of Spt4/5 is universally conserved in evolution, the added functionality of F/E-like complexes has emerged after the split of the bacterial and archaeo-eukaryotic lineages. Interestingly, bacteriophage-encoded antiterminator proteins could, in theory, fulfil an analogous function in the bacterial RNAP.
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