Open AccessA Broad Range of Conformations Contribute to the Solution Ensemble of the Essential Splicing Factor U2AF65
Author(s) -
Jermaine L. Jenkins,
Kholiswa M. Laird,
Clara L. Kielkopf
Publication year - 2012
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/bi300277t
Subject(s) - rna splicing , polypyrimidine tract , splice , chemistry , physics , rna , biology , crystallography , computational biology , genetics , gene
U2AF(65) is essential for pre-mRNA splicing in most eukaryotes. Two consecutive RNA recognition motifs (RRM) of U2AF(65) recognize a polypyrimidine tract at the 3' splice site. Here, we use small-angle X-ray scattering to demonstrate that the tandem U2AF(65) RRMs exhibit a broad range of conformations in the solution ensemble. The majority of U2AF(65) conformations exhibit few contacts between the RRMs, such as observed in the crystal structure. A subpopulation adopts tight inter-RRM contacts, such as independently reported based on paramagnetic relaxation enhancements. These complementary structural methods demonstrate that diverse splice sites have the opportunity to select compact or extended inter-RRM proximities from the U2AF(65) conformational pool.