PDBsum entry 2mjf

Protein binding

PDB id: 2mjf

Contents

Protein chains

40 a.a.

95 a.a.

PDB id:

2mjf

Name:

Protein binding

Title:

Solution structure of the complex between the yeast rsa1 and hit1 proteins

Structure:

Ribosome assembly 1 protein. Chain: a. Engineered: yes. Protein hit1. Chain: b. Engineered: yes

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: rsa1, ypl193w. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hit1, yjr055w, j1705.

NMR struc:

20 models

Authors:

M.Quinternet,B.Roth,R.Back,C.Jacquemin,X.Manival

Key ref:

B.Rothé et al. (2014). Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction. Nucleic Acids Res, 42, 10731-10747. PubMed id: 25170085 DOI: 10.1093/nar/gku612

Date:

08-Jan-14 Release date: 10-Sep-14

Protein chain

Q08932  (RSA1_YEAST) -  Ribosome assembly 1 protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 381 a.a.

Struc: 40 a.a.*

Protein chain

P46973  (HIT1_YEAST) -  Protein HIT1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 164 a.a.

Struc: 95 a.a.

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1093/nar/gku612

Nucleic Acids Res 42:10731-10747 (2014)

PubMed id: 25170085

Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.

B.Rothé, J.M.Saliou, M.Quinternet, R.Back, D.Tiotiu, C.Jacquemin, C.Loegler, F.Schlotter, V.Peña, K.Eckert, S.Moréra, A.V.Dorsselaer, C.Branlant, S.Massenet, S.Sanglier-Cianférani, X.Manival, B.Charpentier.

ABSTRACT

Biogenesis of eukaryotic box C/D small nucleolar ribonucleoprotein particles (C/D snoRNPs) involves conserved trans-acting factors, which are proposed to facilitate the assembly of the core proteins Snu13p/15.5K, Nop58p/NOP58, Nop56p/NOP56 and Nop1p/Fibrillarin on box C/D small nucleolar RNAs (C/D snoRNAs). In yeast, protein Rsa1 acts as a platform, interacting with both the RNA-binding core protein Snu13 and protein Pih1 of the Hsp82-R2TP chaperone complex. In this work, a proteomic approach coupled with functional and structural studies identifies protein Hit1 as a novel Rsa1p-interacting partner involved in C/D snoRNP assembly. Hit1p contributes to in vivo C/D snoRNA stability and pre-RNA maturation kinetics. It associates with U3 snoRNA precursors and influences its 3'-end processing. Remarkably, Hit1p is required to maintain steady-state levels of Rsa1p. This stabilizing activity is likely to be general across eukaryotic species, as the human protein ZNHIT3(TRIP3) showing sequence homology with Hit1p regulates the abundance of NUFIP1, the Rsa1p functional homolog. The nuclear magnetic resonance solution structure of the Rsa1p317-352-Hit1p70-164 complex reveals a novel mode of protein-protein association explaining the strong stability of the Rsa1p-Hit1p complex. Our biochemical data show that C/D snoRNAs and the core protein Nop58 can interact with the purified Snu13p-Rsa1p-Hit1p heterotrimer.