Chemical shift assignments of a minimal Rna14p/Rna15p heterodimer from the yeast cleavage factor IA complex.
The two yeast proteins Rna14p and Rna15p form part of the cleavage/polyadenylation factor IA (CF IA) complex that is involved in the 3' processing of pre-mRNA. Association of the two proteins is mediated by a small C-terminal peptide from Rna14p and a region in Rna15p that corresponds to the hinge domain first identified within the human orthologue. Here I report the (1)H, (13)C and (15)N spectral assignments for a bacterially co-expressed heterodimer of Rna14p/Rna15p. Further analysis of secondary chemical shifts reveals that both peptides are predominantly α-helical within the complex.
Mackereth
Cameron D
CD
Institut Européen de Chimie et Biologie, Pessac, France. c.mackereth@iecb.u-bordeaux.fr
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D039221:mRNA Cleavage and Polyadenylation Factors / Q000737:chemistry*
D046912:Multiprotein Complexes; D029701:Saccharomyces cerevisiae Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; C512638:RNA14 protein, S cerevisiae; C512635:RNA15 protein, S cerevisiae