Rpa43 and its partners in the yeast RNA polymerase I transcription complex
Rpa43 and its partners in the yeast RNA polymerase I transcription complex
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DOI：
10.1016/j.febslet.2011.09.011
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发表时间：
2011-11-04
期刊：
影响因子：
3.5
通讯作者：
Thuriaux, Pierre
中科院分区：
文献类型：
--
作者：
Beckouet, Frederic;Mariotte-Labarre, Sylvie;Thuriaux, Pierre
Rpa 43/Rpa 14茎从RNA聚合酶I（RNAPI）突出，与Rpb 7/Rpb 4（RNAPII）、Rpc 25/Rpc 17（RNAPIII）和RpoE/RpoF（古细菌）同源。在真菌和脊椎动物中，Rpa 43含有亲水结构域，其大小约为Rpa 43的一半，但这些结构域在粟酒裂殖酵母和大多数其他真核生物谱系中缺乏。在酿酒酵母中，它们可以丢失而几乎没有或没有生长效应，如缺失作图和与裂殖酵母的结构域交换所示，但与rpa 12 D、rpa 34 D或rpa 49 D遗传相互作用，缺乏对转录延长重要的非必需亚基。双杂交数据和其他遗传证据表明，Rpa 43直接结合Spt 5，这是一种也在RNAPI II依赖性转录中起作用的RNAPI延伸因子，并且还可能与核小体伴侣Spt 6相互作用。RPA 43通过两个杂交体与SPT 6物理相互作用（查看相互作用）通过荧光显微镜观察HMO 1和SPT 6共定位（查看相互作用）RPA 43通过两个混合物与RPA 14物理相互作用（查看交互）RPA 43通过两个混合与SPT 5进行物理交互（View interaction）HMO 1和SPT 5通过荧光显微镜共定位（View interaction）（C）2011欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
An Rpa43/Rpa14 stalk protrudes from RNA polymerase I (RNAPI), with homology to Rpb7/Rpb4 (RNAPII), Rpc25/Rpc17 (RNAPIII) and RpoE/RpoF (archaea). In fungi and vertebrates, Rpa43 contains hydrophilic domains forming about half of its size, but these domains lack in Schizosaccharomyces pombe and most other eukaryote lineages. In Saccharomyces cerevisiae, they can be lost with little or no growth effect, as shown by deletion mapping and by domain swapping with fission yeast, but genetically interact with rpa12D, rpa34D or rpa49D, lacking non-essential subunits important for transcript elongation. Two-hybrid data and other genetic evidence suggest that Rpa43 directly bind Spt5, an RNAPI elongation factor also acting in RNAPII-dependent transcription, and may also interact with the nucleosomal chaperone Spt6.Structured summary of protein interactions:RPA43 physically interacts with SPT6 by two hybrid (View interaction)HMO1 and SPT6 colocalize by fluorescence microscopy (View interaction)RPA43 physically interacts with RPA14 by two hybrid (View interaction)RPA43 physically interacts with SPT5 by two hybrid (View interaction)HMO1 and SPT5 colocalize by fluorescence microscopy (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.