Plc1p is required for SAGA recruitment and derepression of Sko1p-regulated genes.
Plc1p is required for SAGA recruitment and derepression of Sko1p-regulated genes.
复制标题
Plc1p 是 SAGA 招募和 Sko1p 调节基因去抑制所必需的。
DOI：
10.1091/mbc.e06-10-0946
复制
发表时间：
2007
影响因子：
3.3
通讯作者：
Vancura,Ales
中科院分区：
文献类型：
--
作者：
Guha,Nilanjan;Desai,Parima;Vancura,Ales
在酿酒酵母中，许多可诱导的基因受Sko 1 p-Ssn 6p-Tup 1 p复合物的调控。在渗透压休克时，MAP激酶Hog 1 p与该复合物结合，磷酸化Sko 1 p，并将其转化为随后募集Swi/Snf和佐贺复合物的激活剂。我们已经发现，磷脂酶C（PLC 1编码的Plc 1 p）是必需的去阻遏的Sko 1 p-Ssn 6p-Tup 1 p控制的细胞凋亡诱导基因在渗透压休克。尽管plc 1 Δ突变影响了渗透压休克后前起始复合物的组装，但它不影响Hog 1 p和Swi/Snf复合物在这些启动子上的募集。然而，Plc 1 p促进渗透压休克诱导的佐贺复合物的募集。与plc 1 Δ细胞一样，佐贺突变体对肿瘤敏感，并显示肿瘤诱导基因的表达受损。在plc 1 Δ细胞中，佐贺与Sko 1 p-Ssn 6p-Tup 1 p抑制的启动子的结合减少与组蛋白乙酰化减少无关。然而，佐贺在这些启动子处起作用以促进TATA结合蛋白的募集。因此，结果提供的证据表明，Plc 1 p和肌醇多磷酸影响去阻遏的Sko 1 p-Ssn 6p-Tup 1 p控制的基因的机制，涉及招聘的佐贺复合物和TATA结合蛋白。
InSaccharomyces cerevisiae, many osmotically inducible genes are regulated by the Sko1p-Ssn6p-Tup1p complex. On osmotic shock, the MAP kinase Hog1p associates with this complex, phosphorylates Sko1p, and converts it into an activator that subsequently recruits Swi/Snf and SAGA complexes. We have found that phospholipase C (Plc1p encoded byPLC1) is required for derepression of Sko1p-Ssn6p-Tup1p–controlled osmoinducible genes upon osmotic shock. Althoughplc1Δ mutation affects the assembly of the preinitiation complex after osmotic shock, it does not affect the recruitment of Hog1p and Swi/Snf complex at these promoters. However, Plc1p facilitates osmotic shock–induced recruitment of the SAGA complex. Likeplc1Δ cells, SAGA mutants are osmosensitive and display compromised expression of osmotically inducible genes. The reduced binding of SAGA to Sko1p-Ssn6p-Tup1p–repressed promoters inplc1Δ cells does not correlate with reduced histone acetylation. However, SAGA functions at these promoters to facilitate recruitment of the TATA-binding protein. The results thus provide evidence that Plc1p and inositol polyphosphates affect derepression of Sko1p-Ssn6p-Tup1p–controlled genes by a mechanism that involves recruitment of the SAGA complex and TATA-binding protein.