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首页> 美国卫生研究院文献>Genetics >Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae
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Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae

机译：陪伴伴侣：陪伴伴侣Cpr7在酿酒酵母中调节Hsp90功能的作用。

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摘要

Heat-shock protein 90 () of Saccharomyces cerevisiae is an abundant essential eukaryotic molecular chaperone involved in the activation and stabilization of client proteins, including several transcription factors and oncogenic kinases. undergoes a complex series of conformational changes and interacts with partner co-chaperones such as , , , and as it binds and hydrolyzes ATP. In the absence of nucleotide, is dimerized only at the carboxy-terminus. In the presence of ATP, also dimerizes at the amino-terminus, creating a binding site for . Truncation of a charged linker region of yeast (Δlinker) was known to disrupt the ability of to undergo amino-terminal dimerization and bind . We found that yeast expressing Δlinker constructs exhibited a specific synthetic lethal phenotype in cells lacking . The isolated tetratricopeptide repeat domain of was both necessary and sufficient for growth in those strains. href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr6 and href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr7 stably bound the carboxy-terminus of wild-type href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82 only in the presence of nonhydrolyzable ATP and formed an href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82–href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr6–href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr7 ternary complex. However, in cells expressing href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82Δlinker or lacking href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">CPR7, href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr6 was able to bind href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82 in the presence or absence of nucleotide. Overexpression of href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000359" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">CNS1, but not of other co-chaperones, in href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">cpr7 cells restored nucleotide-dependent href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82–href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr6 interaction. Together, our results suggest that the in vivo functions of href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr7 include modulating href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp90 conformational changes, mediating proper signaling of the nucleotide-bound state to the carboxy-terminus of href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82, or regulating href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Hsp82–href="http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206" data-ga-action="click_feat_suppl" ref="reftype=extlink&article-id=3389976&issue-id=211838&journal-id=301&FROM=Article%7CFront%20Matter&TO=External%7CLink%7CURI" target="_blank">Cpr6 interaction.
机译：酿酒酵母的热激蛋白90（）是一种丰富的必不可少的真核分子伴侣，参与客户蛋白的激活和稳定化，包括几种转录因子和致癌激酶。经历一系列复杂的构象变化，并与诸如，，的伴侣伴侣分子相互作用，并与ATP结合并水解。在没有核苷酸的情况下，仅在羧基末端二聚。在ATP存在的情况下，其氨基末端也会二聚，形成的结合位点。已知酵母的带电荷连接子区域（Δ连接子）的截短会破坏氨基末端二聚化和结合的能力。我们发现，酵母表达Δ连接器的结构表现出细胞缺乏特定的合成致死表型。分离的四糖肽重复结构域对于在那些菌株中生长既是必需的又是足够的。 href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206” data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal -id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Cpr6 和href =” http://www.yeastgenome.org/cgi-bin/locus。 fpl？dbid = S000003793“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank “> Cpr7 稳定地绑定了野生型href =” http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161“的羧基端“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI” target =“ _ blank”> Hsp82 不可水解的ATP，并形成href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161” data-ga-action =“ click_feat_suppl” ref =“ reftype = e xtlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Hsp82 – href =” http：//www.yeastgenome .org / cgi-bin / locus.fpl？dbid = S000004206“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External ％7CLink％7CURI“ target =” _ blank“> Cpr6 – href =” http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793“ data-ga-action = “ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI” target =“ _ blank”> Cpr7 三元复合体。但是，在表示href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161”的单元格中，data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Hsp82 Δlinker或缺少href =” http://www.yeastgenome.org /cgi-bin/locus.fpl?dbid=S000003793“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink ％7CURI“ target =” _ blank“> CPR7 ，href =” http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206“ data-ga-action =” click_feat_suppl “ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Cpr6 能够绑定href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161” data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆jo urnal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Hsp82 在存在或不存在核苷酸的情况下。 href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000359”的过表达。data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> CNS1 ，但不包括其他共同伴侣，在href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793” data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> cpr7 细胞恢复了核苷酸依赖性href =” http://www.yeastgenome.org/ cgi-bin / locus.fpl？dbid = S000006161“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％ 7CURI“ target =” _ blank“> Hsp82 – href =” http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206“ data-ga-action =” click_feat_suppl“ ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI” target =“ _ blank”> Cpr6 交互。在一起，我们的结果表明href =“ http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003793”的体内功能data = ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Cpr7 包括调制href =” http：// www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000006161“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％ 20Matter＆TO = External％7CLink％7CURI“ target =” _ blank“> Hsp90 构象变化，介导核苷酸结合状态正确传递信号给href =” http://www.yeastgenome.com.cn]的羧基末端org / cgi-bin / locus.fpl？dbid = S000006161“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％ 7CLink％7CURI“ target =” _ blank“> Hsp82 ，或规范href =” http：//www.yeast基因组.org / cgi-bin / locus.fpl？dbid = S000006161“ data-ga-action =” click_feat_suppl“ ref =” reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO =外部％7CLink％7CURI“ target =” _ blank“> Hsp82 – href =” http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004206“ data-ga-action =“ click_feat_suppl” ref =“ reftype = extlink＆article-id = 3389976＆issue-id = 211838＆journal-id = 301＆FROM = Article％7CFront％20Matter＆TO = External％7CLink％7CURI” target =“ _ blank”> Cpr6 互动。

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