Association of yeast SAP1, a novel member of the ‘AAA’ ATPase family of proteins, with the chromatin protein SIN1

FEBS Letters

Yona, Eyal¹  Katcoff, Don J.¹  Bangio, Haim¹  Liberzon, Arthur¹  Shpungin, Sally¹ 

[1]Department of Life Sciences, Bar Ilan University, Ramat Gan 52900, Israel

关键词: Chromatin structure;    Protein-protein interaction;    Transcriptional repression;    AAA family of ATPases;    SIN1/SPT2;    SWI/SNF complex;    Saccharomyces cerevisiae;    AAA;    TPases associated with diverse cellular activities;    ORF;    open reading frame;    UAS;    upstream activating sequence;   

DOI  :  10.1016/0014-5793(96)00500-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The yeast SIN1 protein is a nuclear protein that together with other proteins behaves as a transcriptional repressor of a family of genes. In addition, sin1 mutants are defective in proper mitotic chromosome segregation. In an effort to understand the basis for these phenotypes, we employed the yeast two-hybrid system to identify proteins that interact with SIN1 in vivo. Here, we demonstrate that SAP1, a novel protein belonging to the ‘AAA’ family of ATPases, is able to directly interact with SIN1. Furthermore, we show, using recombinant molecules in vitro, that a short 27 amino acid sequence near the N-terminal of SIN1 is sufficient to bind SAP1. Previous experiments defined different domains of SIN that interact with other proteins and with DNA. The C-terminal domain of SIN1 was shown to be responsible for interaction with a protein that binds the regulatory region of HO, a gene whose transcription is repressed by SIN1. The central ‘HMG1-like region’ of SIN1 binds DNA, while the N-terminal of SIN1 can bind CDC23, a protein that regulates chromosome segregation. These data, taken together with the results presented here, suggest that SIN1 is a multifunctional chromatin protein that can interact with a number of different proteins that are involved in several different cellular functions.

【 授权许可】

Unknown