(1)H, (15)N and (13)C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex

Xavier Manival; Clémence Jacquemin; Bruno Charpentier; Marc Quinternet

doi:10.1007/s12104-014-9547-1

(1)H, (15)N and (13)C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex

Biomol NMR Assign. 2015 Apr;9(1):71-3. doi: 10.1007/s12104-014-9547-1. Epub 2014 Feb 4.

Authors

Xavier Manival¹, Clémence Jacquemin, Bruno Charpentier, Marc Quinternet

Affiliation

¹ Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS, Université de Lorraine, Biopôle de l'Université de Lorraine, Campus Biologie Santé, 9 avenue de la forêt de Haye, CS 50184, 54505, Vandœuvre-lès-Nancy, France.

PMID: 24493341
DOI: 10.1007/s12104-014-9547-1

Abstract

We report the nearly complete (1)H, (15)N and (13)C resonance assignment of the complex formed by the C-terminal domains of Pih1 and Tah1 from S. cerevisiae and evidence the folding ability of Tah1 under complex formation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Molecular Chaperones / chemistry*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular*
Nuclear Proteins / chemistry*
Protein Structure, Tertiary
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins / chemistry*

Substances

Molecular Chaperones
Nuclear Proteins
PIH1 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
Tah1 protein, S cerevisiae