Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p.

Ge Yu, Yu Zhao, Shaoxiong Tian, Jay Rai, Huan He, John Spear, Duncan Sousa, Jinbo Fan, Hong-Guo Yu, Scott M Stagg, Hong Li

Scientific reports 2019 Dec 27

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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.

Citation

Ge Yu, Yu Zhao, Shaoxiong Tian, Jay Rai, Huan He, John Spear, Duncan Sousa, Jinbo Fan, Hong-Guo Yu, Scott M Stagg, Hong Li. Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p. Scientific reports. 2019 Dec 27;9(1):20228