Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p

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作者
Ge Yu
Yu Zhao
Shaoxiong Tian
Jay Rai
Huan He
John Spear
Duncan Sousa
Jinbo Fan
Hong-Guo Yu
Scott M. Stagg
Hong Li
机构
[1] Florida State University,Department of Chemistry and Biochemistry
[2] Institute of Molecular Biophysics,Department of Biological Science
[3] Florida State University,undefined
[4] Florida State University,undefined
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Scientific Reports | / 9卷
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摘要
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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