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.
Biomol NMR Assign
Date: Oct. 22, 2010
PubMed ID: 20967574
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