A split motor domain in a cytoplasmic dynein

A split motor domain in a cytoplasmic dynein
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细胞质动力蛋白中的分裂运动结构域

DOI:
10.1093/emboj/20.18.5091
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发表时间:
2001
期刊:
The EMBO Journal
影响因子:
--
通讯作者:
G. Steinberg
G. Steinberg
中科院分区:
--
文献类型:
--
作者:
A. Straube;W. Enard;Al Berner;Roland Wedlich;R. Kahmann;G. Steinberg

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动力蛋白的重链形成一个球状运动结构域,该结构域与ATP切割区和微管结合位点紧密偶联,将化学能转化为沿着细胞骨架的运动。在这里,我们表明,在真菌玉米黑粉菌,两个基因,dyn 1和dyn 2,编码动力蛋白重链。推定的ATP酶区域由dyn 1提供,而dyn 2包括预测的微管结合位点。这两种基因位于不同的染色体上,被转录成独立的mRNA并被翻译成单独的多肽。Dyn 1和Dyn 2在生长的细胞内共免疫沉淀和共定位,Dyn 1-Dyn 2融合蛋白部分挽救了突变表型,表明两种多肽相互作用形成复合物。在细胞提取物中,Dyn 1-Dyn 2复合物解离,微管亲和纯化表明Dyn 1或相关多肽独立于Dyn 2结合微管。Dyn 1和Dyn 2都是细胞生存所必需的,条件突变体在核迁移、细胞形态发生和微管组织中发挥共同作用,表明Dyn 1-Dyn 2复合物具有多种细胞功能。
The heavy chain of dynein forms a globular motor domain that tightly couples the ATP‐cleavage region and the microtubule‐binding site to transform chemical energy into motion along the cytoskeleton. Here we show that, in the fungus Ustilago maydis, two genes, dyn1 and dyn2, encode the dynein heavy chain. The putative ATPase region is provided by dyn1, while dyn2 includes the predicted microtubule‐binding site. Both genes are located on different chromosomes, are transcribed into independent mRNAs and are translated into separate polypeptides. Both Dyn1 and Dyn2 co‐immunoprecipitated and co‐localized within growing cells, and Dyn1–Dyn2 fusion proteins partially rescued mutant phenotypes, suggesting that both polypeptides interact to form a complex. In cell extracts the Dyn1–Dyn2 complex dissociated, and microtubule affinity purification indicated that Dyn1 or associated polypeptides bind microtubules independently of Dyn2. Both Dyn1 and Dyn2 were essential for cell survival, and conditional mutants revealed a common role in nuclear migration, cell morphogenesis and microtubule organization, indicating that the Dyn1–Dyn2 complex serves multiple cellular functions.
DOI: 10.1101/gr.9.1.27
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期刊: Genetics
影响因子: 3.3
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