The Yeast AAA+ Chaperone Hsp104 Is Part of a Network That Links the Actin Cytoskeleton with the Inheritance of Damaged Proteins
The Yeast AAA+ Chaperone Hsp104 Is Part of a Network That Links the Actin Cytoskeleton with the Inheritance of Damaged Proteins
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DOI：
10.1128/mcb.00201-09
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发表时间：
2009-07-01
影响因子：
5.3
通讯作者：
Bukau, Bernd
中科院分区：
文献类型：
--
作者：
Tessarz, Peter;Schwarz, Michael;Bukau, Bernd
酵母AAA(+)分子伴侣Hsp104对于耐热性的形成和对Pron的遗传是必不可少的。最近，HSP104和肌动蛋白细胞骨架一起被发现参与了碳化蛋白质的不对称分布。在这里，我们通过使用Hsp104的显性-负变异体(HAP/ClpP)来研究Hsp104和肌动蛋白之间的相互作用，该变体降解底物蛋白而不是重塑它们。HAP/ClpP共表达会导致细胞形态和肌动蛋白细胞骨架的缺陷。采用候选方法，我们确定Spa2是极化体复合体的成员，是Hsp104底物。此外，我们提供了将Spa2和Hsp104与细胞质分裂机制成员Hof1联系起来的遗传学证据。Spa2和Hof1基因敲除细胞受到损伤蛋白不对称分布的影响，表明Hsp104、Spa2和Hof1是控制碳化蛋白遗传的网络成员。
The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions. Recently, Hsp104, together with the actin cytoskeleton, has been implicated in the asymmetric distribution of carbonylated proteins. Here, we investigated the interplay between Hsp104 and actin by using a dominant-negative variant of Hsp104 (HAP/ClpP) that degrades substrate proteins instead of remodeling them. Coexpression of HAP/ClpP causes defects in morphology and the actin cytoskeleton. Taking a candidate approach, we identified Spa2, a member of the polarisome complex, as an Hsp104 substrate. Furthermore, we provided genetic evidence that links Spa2 and Hsp104 to Hof1, a member of the cytokinesis machinery. Spa2 and Hof1 knockout cells are affected in the asymmetric distribution of damaged proteins, suggesting that Hsp104, Spa2, and Hof1 are members of a network controlling the inheritance of carbonylated proteins.