Organization of the yeast Zip1 protein within the central region of the synaptonemal complex.
Organization of the yeast Zip1 protein within the central region of the synaptonemal complex.
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DOI：
10.1083/jcb.148.3.417
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发表时间：
2000-02-07
期刊：
影响因子：
--
通讯作者：
Roeder GS
中科院分区：
文献类型：
--
作者：
Dong H;Roeder GS
酵母Zip 1蛋白是联会复合体（SC）中心区域的组分。预测Zip 1形成α-螺旋卷曲螺旋，在NH 2和COOH末端两侧是球状结构域。免疫金标记与域特异性抗Zip 1抗体表明，Zip 1的NH 2-末端结构域位于SC的中心区域的中间，而COOH-末端结构域嵌入在复合物的横向元素。以前的研究表明，Zip 1的过度生产导致两种类型的聚集体，多复合物和网络的组装，这是与染色质无关的。我们的表位作图数据表明，组织内的Zip 1的polycomplex是类似的SC，而组织内的Zip 1网络是根本不同的。从细菌中纯化的Zip 1蛋白在体外组装成二聚体，电子显微镜分析表明，二聚体中的两个单体平行排列并对齐。总之，这些结果表明，两个Zip 1二聚体，躺在头对头，跨越SC的宽度。
The yeast Zip1 protein is a component of the central region of the synaptonemal complex (SC). Zip1 is predicted to form an α-helical coiled coil, flanked by globular domains at the NH2 and COOH termini. Immunogold labeling with domain-specific anti–Zip1 antibodies demonstrates that the NH2-terminal domain of Zip1 is located in the middle of the central region of the SC, whereas the COOH-terminal domain is embedded in the lateral elements of the complex. Previous studies have shown that overproduction of Zip1 results in the assembly of two types of aggregates, polycomplexes and networks, that are unassociated with chromatin. Our epitope mapping data indicate that the organization of Zip1 within polycomplexes is similar to that of the SC, whereas the organization of Zip1 within networks is fundamentally different. Zip1 protein purified from bacteria assembles into dimers in vitro, and electron microscopic analysis demonstrates that the two monomers within a dimer are arranged in parallel and in register. Together, these results suggest that two Zip1 dimers, lying head-to-head, span the width of the SC.
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