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R2TP_TAP-MS - R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein

ABSTRACT: The R2TP/Prefoldin-like (R2TP/PFDL) complex is a cochaperone complex involved in the assembly of a number of critical protein complexes. Here we use multiple target tandem affinity purification (TAP) coupled to mass spectrometry to map out the interaction network around R2TP/PFDL.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Christian Poitras

LAB HEAD: Benoit Coulombe

PROVIDER: PXD006198 | Pride | 2018-10-24

REPOSITORIES: Pride

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			Action	DRS
	F012079.dat	Other
	F012081.dat	Other
	F027876.dat	Other
	F027879.dat	Other
	F027997.dat	Other

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Publications

R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein.

Cloutier Philippe P Poitras Christian C Durand Mathieu M Hekmat Omid O Fiola-Masson Émilie É Bouchard Annie A Faubert Denis D Chabot Benoit B Coulombe Benoit B

Nature communications 20170531

The R2TP/Prefoldin-like (R2TP/PFDL) complex has emerged as a cochaperone complex involved in the assembly of a number of critical protein complexes including snoRNPs, nuclear RNA polymerases and PIKK-containing complexes. Here we report on the use of multiple target affinity purification coupled to mass spectrometry to identify two additional complexes that interact with R2TP/PFDL: the TSC1-TSC2 complex and the U5 small nuclear ribonucleoprotein (snRNP). The interaction between R2TP/PFDL and the ...[more]

PMID: 28561026

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Project description:The R2TP/Prefoldin-like (R2TP/PFDL) complex is a cochaperone complex involved in the assembly of a number of critical protein complexes. Here we use stable isotope labeling with amino acids in cell culture (SILAC) and FLAG tag affinity purification coupled to mass spectrometry to assess whether siRNA-driven knockdown of cofactors or subunits of R2TP/PFDN affects composition of U5 snRNP and TSC complex.

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