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

P Cloutier, C Poitras, M Durand, O Hekmat… - Nature …, 2017 - nature.com
Abstract 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 …

Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI

M Gstaiger, B Luke, D Hess, EJ Oakeley, C Wirbelauer… - Science, 2003 - science.org
Prefoldins (PFDs) are members of a recently identified, small–molecular weight protein
family able to assemble into molecular chaperone complexes. Here we describe an …

The prefoldin bud27 mediates the assembly of the eukaryotic RNA polymerases in an rpb5-dependent manner

MC Mirón-García, AI Garrido-Godino… - PLoS …, 2013 - journals.plos.org
The unconventional prefoldin URI/RMP, in humans, and its orthologue in yeast, Bud27, have
been proposed to participate in the biogenesis of the RNA polymerases. However, this role …

NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins

J Bizarro, M Dodré, A Huttin, B Charpentier… - Nucleic acids …, 2015 - academic.oup.com
The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific
proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs …

TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation

K Klimešová, J Vojáčková, N Radivojević… - Nature …, 2021 - nature.com
U5 snRNP is a complex particle essential for RNA splicing. U5 snRNPs undergo intricate
biogenesis that ensures that only a fully mature particle assembles into a splicing competent …

Analysis of URI nuclear interaction with RPB5 and components of the R2TP/prefoldin-like complex

P Mita, JN Savas, S Ha, N Djouder, JR Yates III… - PLoS …, 2013 - journals.plos.org
Unconventional prefoldin RPB5 Interactor (URI) was identified as a transcriptional repressor
that binds RNA polymerase II (pol II) through interaction with the RPB5/POLR2E subunit …

The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling

A Bergfort, T Hilal, B Kuropka, İA Ilik… - Nucleic Acids …, 2022 - academic.oup.com
Biogenesis of spliceosomal small nuclear ribonucleoproteins (snRNPs) and their recycling
after splicing require numerous assembly/recycling factors whose modes of action are often …

Structure/function analysis of protein–protein interactions developed by the Yeast Pih1 platform protein and its partners in Box C/D snoRNP Assembly

M Quinternet, B Rothé, M Barbier, C Bobo… - Journal of molecular …, 2015 - Elsevier
In eukaryotes, nucleotide post-transcriptional modifications in RNAs play an essential role in
cell proliferation by contributing to pre-ribosomal RNA processing, ribosome assembly and …

The ribosome biogenesis factor yUtp23/hUTP23 coordinates key interactions in the yeast and human pre-40S particle and hUTP23 contains an essential PIN domain

GR Wells, F Weichmann, KE Sloan… - Nucleic Acids …, 2017 - academic.oup.com
Two proteins with PIN endonuclease domains, yUtp24 (Fcf1)/hUTP24 and yUtp23/hUTP23
are essential for early pre-ribosomal (r) RNA cleavages at sites A0, A1/1 and A2/2a in yeast …

[HTML][HTML] Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex

Z Hořejší, L Stach, TG Flower, D Joshi, H Flynn… - Cell reports, 2014 - cell.com
The R2TP cochaperone complex plays a critical role in the assembly of multisubunit
machines, including small nucleolar ribonucleoproteins (snoRNPs), RNA polymerase II, and …