Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.
Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.
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DOI：
10.1038/ncomms13563
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发表时间：
2016-11-24
影响因子：
16.6
通讯作者：
Sinning, Irmgard
中科院分区：
文献类型：
--
作者：
Gumiero, Andrea;Conz, Charlotte;Gese, Genis Valentin;Zhang, Ying;Weyer, Felix Alexander;Lapouge, Karine;Kappes, Julia;von Plehwe, Ulrike;Schermann, Geza;Fitzke, Edith;Woelfle, Tina;Fischer, Tamas;Rospert, Sabine;Sinning, Irmgard
在所有生物体中，共译伴侣协助新生多肽的从头折叠。在酵母中，异二聚体核糖体相关复合体（RAC）与Hsp70同源物Ssb形成独特的伴侣三联体。我们在2.6 Å分辨率下报道了全长Ssb的atp结合开放构象的x射线结构，并在α-螺旋盖结构域（SBDα）中发现了一个带正电的区域，该区域存在于hsp70的Ssb亚家族的所有成员中。突变分析表明，该区域是核糖体结合所必需的。交联表明，Ssb通过与核糖体蛋白和rRNA的接触结合在隧道出口附近，并且特定的接触可以与开放（atp结合）和封闭（adp结合）构象之间的切换相关。综上所述，我们的数据揭示了核糖体上的Ssb动力学如何允许在rac介导的ATP水解激活中与新生链有效相互作用。在酵母中，异二聚体核糖体相关复合体（RAC）与Hsp70蛋白Ssb协同作用，形成独特的伴侣三联体。在这里，作者使用结构和生化方法来阐明翻译和折叠是如何在真核生物中耦合的。
Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformation at 2.6 Å resolution and identify a positively charged region in the α-helical lid domain (SBDα), which is present in all members of the Ssb-subfamily of Hsp70s. Mutational analysis demonstrates that this region is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. Taken together, our data reveal how Ssb dynamics on the ribosome allows for the efficient interaction with nascent chains upon RAC-mediated activation of ATP hydrolysis. In yeast, the heterodimeric ribosome-associated complex (RAC) acts in concert with the Hsp70 protein Ssb, forming a unique chaperone triad. Here the authors use structural and biochemical approaches to shed light on how translation and folding are coupled in eukaryotes.
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影响因子：
3.5
作者：
Dörfel MJ;Lyon GJ
通讯作者：
Lyon GJ
影响因子：
64.5
作者：
Albanèse, V;Yam, AYW;Frydman, J
通讯作者：
Frydman, J
DOI：
10.1073/pnas.0903503106
发表时间：
2009-05-26
影响因子：
11.1
作者：
Bertelsen, Eric B.;Chang, Lyra;Zuiderweg, Erik R. P.
通讯作者：
Zuiderweg, Erik R. P.
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
DOI：
10.1107/s0907444909042073
发表时间：
2010-01
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Chen VB;Arendall WB 3rd;Headd JJ;Keedy DA;Immormino RM;Kapral GJ;Murray LW;Richardson JS;Richardson DC
通讯作者：
Richardson DC