PDBsum entry 2m3f

RNA binding protein

PDB id: 2m3f

Contents

Protein chain

22 a.a.

PDB id:

2m3f

Name:

RNA binding protein

Title:

Nmr structure of rsa1p238-259 from s. Cerevisiae

Structure:

Ribosome assembly 1 protein. Chain: a. Fragment: unp residues 238-259. Engineered: yes

Source:

Synthetic: yes. Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Other_details: strain-atcc 204508/s288c, gene-rsa1, ypl193w

NMR struc:

10 models

Authors:

M.Quinternet,X.Manival

Key ref:

B.Rothé et al. (2014). Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly. Nucleic Acids Res, 42, 2015-2036. PubMed id: 24234454 DOI: 10.1093/nar/gkt1091

Date:

17-Jan-13 Release date: 27-Nov-13

Protein chain

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

Seq: 381 a.a.

Struc: 22 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gkt1091

Nucleic Acids Res 42:2015-2036 (2014)

PubMed id: 24234454

Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.

B.Rothé, R.Back, M.Quinternet, J.Bizarro, M.C.Robert, M.Blaud, C.Romier, X.Manival, B.Charpentier, E.Bertrand, C.Branlant.

ABSTRACT

The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex. However, the nature of the Snu13p/15.5K-Rsa1p/NUFIP interaction and its exact role in snoRNP assembly remained to be elucidated. By using biophysical, molecular and imaging approaches, here, we identify residues needed for Snu13p/15.5K-Rsa1p/NUFIP interaction. By NMR structure determination and docking approaches, we built a 3D model of the Snup13p-Rsa1p interface, suggesting that residues R249, R246 and K250 in Rsa1p and E72 and D73 in Snu13p form a network of electrostatic interactions shielded from the solvent by hydrophobic residues from both proteins and that residue W253 of Rsa1p is inserted in a hydrophobic cavity of Snu13p. Individual mutations of residues in yeast demonstrate the functional importance of the predicted interactions for both cell growth and snoRNP formation. Using archaeal box C/D sRNP 3D structures as templates, the association of Snu13p with Rsa1p is predicted to be exclusive of interactions in active snoRNPs. Rsa1p and NUFIP may thus prevent premature activity of pre-snoRNPs, and their removal may be a key step for active snoRNP production.