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A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65).

ABSTRACT: 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.

SUBMITTER: Jenkins JL

PROVIDER: S-EPMC3447987 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65).

Jenkins Jermaine L JL Laird Kholiswa M KM Kielkopf Clara L CL

Biochemistry 20120619 26

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, s ...[more]

PMID: 22702716

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