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

Research output: Contribution to journalArticle

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 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.

Original languageEnglish (US)
Article number20228
JournalScientific reports
Volume9
Issue number1
DOIs
StatePublished - Dec 1 2019

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p'. Together they form a unique fingerprint.

  • Cite this

    Yu, G., Zhao, Y., Tian, S., Rai, J., He, H., Spear, J., Sousa, D., Fan, J., Yu, H. G., Stagg, S. M., & Li, H. (2019). Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p. Scientific reports, 9(1), [20228]. https://doi.org/10.1038/s41598-019-56712-4