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-Structure paper
Title | Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p. |
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Journal, issue, pages | Sci Rep, Vol. 9, Issue 1, Page 20228, Year 2019 |
Publish date | Dec 27, 2019 |
![]() | Ge Yu / Yu Zhao / Shaoxiong Tian / Jay Rai / Huan He / John Spear / Duncan Sousa / Jinbo Fan / Hong-Guo Yu / Scott M Stagg / Hong Li / ![]() |
PubMed Abstract | The AAA + ATPase R2TP complex facilitates assembly of a number of ribonucleoprotein particles (RNPs). Although the architecture of R2TP is known, its molecular basis for acting upon multiple RNPs ...The AAA + ATPase R2TP complex facilitates assembly of a number of ribonucleoprotein particles (RNPs). Although the architecture of R2TP is known, its molecular basis for acting upon multiple RNPs remains unknown. In yeast, the core subunit of the box C/D small nucleolar RNPs, Nop58p, is the target for R2TP function. In the recently observed U3 box C/D snoRNP as part of the 90 S small subunit processome, the unfolded regions of Nop58p are observed to form extensive interactions, suggesting a possible role of R2TP in stabilizing the unfolded region of Nop58p prior to its assembly. Here, we analyze the interaction between R2TP and a Maltose Binding Protein (MBP)-fused Nop58p by biophysical and yeast genetics methods. We present evidence that R2TP interacts largely with the unfolded termini of Nop58p. Our results suggest a general mechanism for R2TP to impart specificity by recognizing unfolded regions in its clients. |
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Methods | EM (single particle) |
Resolution | 8.9 Å |
Structure data | ![]() EMDB-20905: |
Source |
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