The H-1, C-13 and N-15 backbone and side-chain assignment of the RRM domain of SC35, a regulator of pre-mRNA splicing

作者：Clayton Jonathan C; Phelan Marie; Goult Benjamin T; Hautbergue Guillaume M; Wilson Stuart A; Lian Lu Yun^*

来源：Biomolecular NMR Assignments, 2011, 5(1): 7-10.

DOI：10.1007/s12104-010-9254-5

• SC35
• mRNA splicing
• RRM domain
• SFRS2
• PR264
• Splicing factor
• Arginine/serine-rich 2
• NMR

The serine-arginine rich family of proteins play important roles in the regulation of both constitutive and alternative splicing. SC35 (also known as SFRS2 and PR264) is a member of this family and contains one RNA recognition motif (RRM domain) and a RS domain at the C-terminus which is enriched with arginine and serine residues. SC35 is specifically involved in major regulatory pathways for cell proliferation and cell cycle progression. Determining the structure of SC35 would enable greater understanding of how its structure relates to its many functions. Complete H-1, C-13 and N-15 assignments of the RRM domain of SC35 are presented. The assignments were obtained using 2D heteronuclear and 3D triple-resonance experiments with the uniformly [N-15,C-13]-labelled protein. The chemical shifts are used to predict the 3-dimensional structure of this RRM domain in the absence of RNA.

• 出版日期2011-4