(1)H, (15)N and (13)C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex.
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.
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.
Xavier
X
Manival
Clémence
C
Jacquemin
Bruno
B
Charpentier
Marc
M
Quinternet
D000595:Amino Acid Sequence; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009687:Nuclear Proteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
D018832:Molecular Chaperones; D009687:Nuclear Proteins; C497702:PIH1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C571197:Tah1 protein, S cerevisiae