A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition

Article Abstract:

A branchpoint sequence binding protein (BBP) has been identified in yeast. Cooperative interaction between the mammalian splicing factor U2AF65 and mBBP/SF1 is helpful to branchpoint region recognition. U2AF65 binds to the polypyrimidine (PY) tract, which is adjacent. The cooperative RNA binding aids in initial recognition of the branchpoint sequence (BPS) in pre-mRNA splicing. A branchpoint sequence-polypyrimidine tract-containing RNA is involved. The third RNA-binding domain (RBD) of U2AF65 is required for the two proteins to interact, with or without RNA.

Analysis, Genetic aspects, Molecular biology, Protein research, Branched chain amino acids

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The splicing factor BBP interacts specificically with the pre-mRNA branchpoint sequence UACUAAC

Article Abstract:

Ultra-violet (UV) cross-linking techniques were utilized to characterize the direct association between the branchpoint bridging protein (BBP) yeast splicing factor and the pre-messenger RNA (mRNA). Ribonuclease T1 digestion and specific immunoprecipitation indicated the ability of BBP to form UV cross-links to the pre-mRNA near the pre-mRNA branchpoint sequence during commitment-complex assembly. Furthermore, recombinant murine BBP recognized the UACUAAC sequence within the commitment complex.

Nucleoproteins, Carrier proteins, Transport proteins

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Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing

Article Abstract:

The splicing factor hSlu7 is necessary for structural alteration processes prior to step II splicing activity. Late in the splicing pathway of step I, hSlu7 associates with the spliceosome before recognition of the step II splice site. Although hSlu7 has a different structure than spliceosomal complexes, it acts as a functional intermediate between catalytic splicing steps.

United States, RNA splicing

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