Molecular anatomy of the beta' subunit of the E. coli RNA polymerase: identification of regions involved in polymerase assembly.
Molecular anatomy of the beta' subunit of the E. coli RNA polymerase: identification of regions involved in polymerase assembly.
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大肠杆菌 RNA 聚合酶 β 亚基的分子解剖学：鉴定参与聚合酶组装的区域。
DOI：
10.1046/j.1365-2443.1996.700269.x
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Krakow,JS
中科院分区：
文献类型：
--
作者：
Luo,J;Sharif,KA;Jin,R;Fujita,N;Ishihama,A;Krakow,JS
背景:你。coliRNA聚合酶是一种多亚基酶，存在两种不同的形式：催化活性核心酶（α2ββ′）和启动子选择性全酶（α2ββ′σ）。单个亚基正确组装成核心酶或全酶对于酶的功能至关重要。结果：在重组条件下，在靠近中心或C端截短的突变β蛋白能够形成稳定的核心酶样复合物。缺乏201-477氨基酸之间区域的突变体β′蛋白不能形成全酶复合物，但保留了形成核心酶复合物的能力。自由β′亚基与自由σ亚基相互作用形成稳定的β′σ亚基。从β '亚基中去除氨基酸201-477强烈干扰了这种相互作用。结论：β′亚基的N端区参与了核心酶的组装。β′上201和477氨基酸之间的区域可能直接或间接参与β′亚基与σ亚基的相互作用。
Background: TheE. coliRNA polymerase is a multisubunit enzyme, which is present in two different forms: the catalytic competent core enzyme (α2ββ ′) and the promoter selective holoenzyme (α2ββ ′σ). Correct assembly of individual subunits into core or holoenzyme is essential for the function of this enzyme.Results: Mutant β ′ proteins truncated near the centre or at the C‐terminus were able to form stable core enzyme‐like complexes under reconstitution conditions. Mutant β ′ proteins lacking the region between amino acids 201–477 failed to form holoenzyme complexes while retaining the ability to form core enzyme complexes. Furthermore, free β ′ subunit interacted with free σ subunit to form a stable β ′σ subassembly. Removal of amino acids 201–477 from the β ′ subunit strongly interfered with this interaction.Conclusion: Our results suggest that the N‐terminal region of the β ′ subunit is involved in the assembly of core enzyme. The region between amino acids 201 and 477 on β ′ may be directly or indirectly involved in the interaction between the β ′ subunit and the σ subunit.