Sin1的C末端结构域在酵母中与SWI-SNF复合物相互作用。
The C-terminal domain of Sin1 interacts with the SWI-SNF complex in yeast.
作者信息
Pérez-Martín J, Johnson A D
机构信息
Department of Microbiology and Immunology, University of California, San Francisco, California 94143-0414, USA.
出版信息
Mol Cell Biol. 1998 Jul;18(7):4157-64. doi: 10.1128/MCB.18.7.4157.
Abstract
In the yeast Saccharomyces cerevisiae, the SWI-SNF complex has been proposed to antagonize the repressive effects of chromatin by disrupting nucleosomes. The SIN genes were identified as suppressors of defects in the SWI-SNF complex, and the SIN1 gene encodes an HMG1-like protein that has been proposed to be a component of chromatin. Specific mutations (sin mutations) in both histone H3 and H4 genes produce the same phenotypic effects as do mutations in the SIN1 gene. In this study, we demonstrate that Sin1 and the H3 and H4 histones interact genetically and that the C terminus of Sin1 physically associates with components of the SWI-SNF complex. In addition, we demonstrate that this interaction is blocked in the full-length Sin1 protein by the N-terminal half of the protein. Based on these and additional results, we propose that Sin1 acts as a regulatable bridge between the SWI-SNF complex and the nucleosome.
摘要
在酿酒酵母中，SWI-SNF复合物被认为可通过破坏核小体来对抗染色质的抑制作用。SIN基因被鉴定为SWI-SNF复合物缺陷的抑制因子，SIN1基因编码一种类似HMG1的蛋白质，该蛋白质被认为是染色质的一个组成部分。组蛋白H3和H4基因中的特定突变（sin突变）产生的表型效应与SIN1基因中的突变相同。在本研究中，我们证明Sin1与H3和H4组蛋白存在遗传相互作用，并且Sin1的C末端与SWI-SNF复合物的组分存在物理关联。此外，我们证明这种相互作用在全长Sin1蛋白中被该蛋白的N端部分所阻断。基于这些及其他结果，我们提出Sin1作为SWI-SNF复合物与核小体之间的一个可调节桥梁发挥作用。
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