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Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p.

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.

SUBMITTER: Yu G

PROVIDER: S-EPMC6934851 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p.

Yu Ge G Zhao Yu Y Tian Shaoxiong S Rai Jay J He Huan H Spear John J Sousa Duncan D Fan Jinbo J Yu Hong-Guo HG Stagg Scott M SM Li Hong H

Scientific reports 20191227 1

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 poss ...[more]

PMID: 31882871

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