Zip1-induced changes in synaptonemal complex structure and polycomplex assembly.
Zip1-induced changes in synaptonemal complex structure and polycomplex assembly.
复制标题
Zip1诱导的突触复合物结构和多复合物组件的变化。
DOI：
10.1083/jcb.128.4.455
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发表时间：
1995-02
影响因子：
7.8
通讯作者：
Roeder, G S
中科院分区：
文献类型：
--
作者：
Sym, M;Roeder, G S
酵母Zip1蛋白是联会复合体（SC）的组成部分，联会复合体是减数分裂期间沿着染色体长度发现的精细大分子结构。增加预测的卷曲螺旋区域的长度的ZIP1蛋白的突变表明，ZIP1影响SC的宽度。ZIP1基因的过表达导致在细胞核中发现的两种不同类型的高阶结构的形成，但与染色质无关。其中一种结构类似于在许多生物体中观察到的多复合物，被认为是SC组分的聚集体。第二种类型的结构，我们称之为“网络”，不像任何以前确定的SC相关的结构。聚合复合物和网络的组装可以独立于Hop1或Red1蛋白而发生，Hop1或Red1蛋白被认为是SC组分。我们的研究结果表明，Zip1是SC的中心区域的一个结构组成部分。更具体地说，我们推测，Zip1是一个组成部分的横向丝，位于垂直于复合物的长轴。
The yeast Zip1 protein is a component of the synaptonemal complex (SC), which is an elaborate macromolecular structure found along the lengths of chromosomes during meiosis. Mutations that increase the length of the predicted coiled coil region of the Zip1 protein show that Zip1 influences the width of the SC. Overexpression of the ZIP1 gene results in the formation of two distinct types of higher order structures that are found in the nucleus, but not associated with chromatin. One of these structures resembles the polycomplexes that have been observed in many organisms and are thought to be aggregates of SC components. The second type of structure, which we have termed "networks," does not resemble any previously identified SC-related structure. Assembly of both polycomplexes and networks can occur independently of the Hop1 or Red1 protein, which are thought to be SC components. Our results demonstrate that Zip1 is a structural component of the central region of the SC. More specifically, we speculate that Zip1 is a component of the transverse filaments that lie perpendicular to the long axis of the complex.