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Chaperone-mediated pathway of proteasome regulatory particle assembly

机译：伴侣介导的蛋白酶体调控颗粒组装途径

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摘要

The proteasome is a protease that controls diverse processes in eukaryotic cells. Its regulatory particle (RP) initiates the degradation of ubiquitin-protein conjugates by unfolding the substrate and translocating it into the proteasome core particle (CP) to be degraded. The RP has 19 subunits, and their pathway of assembly is not understood. Here we show that in the yeast Saccharomyces cerevisiae three proteins are found associated with RP but not with the RP-CP holoenzyme: Nas6, Rpnl4 and Hsm3. Mutations in the corresponding genes confer proteasome loss-of-function pheno-types, despite their virtual absence from the holoenzyme. These effects result from deficient RP assembly. Thus, Nas6, Rpnl4 and Hsm3 are RP chaperones. The RP contains six ATPases-the Rpt proteins-and each RP chaperone binds to the carboxy-terminal domain of a specific Rpt. We show in an accompanying study2 that RP assembly is templated through the Rpt C termini, apparently by their insertion into binding pockets in the CP. Thus, RP chaperones may regulate proteasome assembly by directly restricting the accessibility of Rpt C termini to the CP. In addition, competition between the RP chaperones and the CP for Rpt engagement may explain the release of RP chaperones as proteasomes mature.
机译：蛋白酶体是控制真核细胞中各种过程的蛋白酶。它的调节颗粒（RP）通过展开底物并将其转移到待降解的蛋白酶体核心颗粒（CP）中来引发泛素-蛋白质共轭物的降解。 RP有19个亚基，其组装途径尚不清楚。在这里我们显示，在酿酒酵母中，发现三种蛋白质与RP相关，但与RP-CP全酶无关：Nas6，Rpnl4和Hsm3。尽管相应的基因实际上缺乏全酶，但相应基因中的突变却赋予了蛋白酶体功能丧失的表型。这些影响是由于RP组装不足所致。因此，Nas6，Rpn14和Hsm3是RP伴侣。 RP包含六个ATPases-Rpt蛋白-每个RP伴侣均结合至特定Rpt的羧基末端结构域。我们在随附的研究中显示，RP组装通过Rpt C末端进行模板化，显然是通过将其插入CP的结合口袋中来完成的。因此，RP分子伴侣可以通过直接限制Rpt C末端对CP的可达性来调节蛋白酶体的组装。此外，RP伴侣和CP之间的Rpt参与竞争可能解释了蛋白酶体成熟时RP伴侣的释放。

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  • 来源
    《Nature》 |2009年第7248期|861-865|共5页
  • 作者

    Jeroen Roelofs; Soyeon Park; Wilhelm Haas; Geng Tian; Fiona E. McAllister; Ying Huo; Byung-Hoon Lee; Fan Zhang; Yigong Shi; Steven P. Gygi; Daniel Finley;

  • 作者单位

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA;

    Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

    Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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