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同源结构域蛋白α2的羧基末端尾巴是与另一种同源结构域蛋白发挥功能所必需的。

The carboxy-terminal tail of the homeo domain protein alpha 2 is required for function with a second homeo domain protein.

作者信息

Mak A, Johnson A D

机构信息

Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0502.

出版信息

Genes Dev. 1993 Oct;7(10):1862-70. doi: 10.1101/gad.7.10.1862.

Abstract

The homeo domain protein alpha 2 from Saccharomyces cerevisiae has two roles in the a/alpha cell: With MCM1, alpha 2 turns off transcription of a-specific genes; with a1 (a second homeo domain protein), alpha 2 represses transcription of haploid-specific genes. From the carboxy-terminal side of the alpha 2 homeo domain extends an unstructured 22-amino-acid residue tail. In this paper we show that the carboxy-terminal tail of alpha 2 is required for formation of a stable a1/alpha 2-operator complex and is thus required for a1/alpha 2-mediated repression of transcription. In contrast, the tail is dispensable for alpha 2/MCM1-mediated repression. These results indicate that a short, unstructured tail mediates the interaction between two homeo domain proteins.

摘要

来自酿酒酵母的同源结构域蛋白α2在a/α细胞中具有两种作用:与MCM1一起,α2关闭a特异性基因的转录;与a1(另一种同源结构域蛋白)一起,α2抑制单倍体特异性基因的转录。从α2同源结构域的羧基末端延伸出一条无结构的22个氨基酸残基的尾巴。在本文中,我们表明α2的羧基末端尾巴是形成稳定的a1/α2-操纵子复合物所必需的,因此也是a1/α2介导的转录抑制所必需的。相比之下,该尾巴对于α2/MCM1介导的抑制作用是可有可无的。这些结果表明,一条短的、无结构的尾巴介导了两种同源结构域蛋白之间的相互作用。

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