Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 ave sequence, structural, and functional homologs and promote RNA polymerase assembly
Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 ave sequence, structural, and functional homologs and promote RNA polymerase assembly
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DOI：
10.1073/pnas.98.3.892
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发表时间：
2001-01-30
影响因子：
11.1
通讯作者：
Severinov, K
中科院分区：
文献类型：
--
作者：
Minakhin, L;Bhagat, S;Severinov, K
细菌DNA依赖的RNA聚合酶（RNAP）有β 'β α（1）α（11）ω亚基组成。我们表明，w是同源的序列和结构的RPB 6，一个重要的亚基共享真核RNAP I，II和III。在大肠杆菌中，ω的过量生产抑制了由RNAP最大亚基β '的残基1362的取代引起的组装缺陷。在酵母中，RPB 6的过量生产抑制了由RNAP II的最大亚基RPB 1中的等效取代引起的组装缺陷。对细菌RNAP中的ω-β '界面的高分辨率结构分析，以及与酵母RNAP II中的RPB 6-RPB 1界面的比较，证实了结构关系，并提出了ω和RPB 6在促进RNAP组装中的作用的“闭锁”机制。
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'beta alpha (1)alpha (11)omega The role of omega has been unclear. We show that w is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.