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Papers In Press, published online ahead of print April 23, 2002
Lung biology Research, Hospital for Sick Children, Toronto, Ontario M5G 1X8
Corresponding Author: jhu{at}sickkids.ca
Human splicing factors Hprp3p and Hprp4p are associated with the U4/U6 small nuclear ribonucleoprotein particle (snRNP), which is essential for the assembly of an active spliceosome. Currently, little is known about the specific roles of these factors in splicing. In this study, we characterized the molecular interaction between Hprp3p and Hprp4p. Constructs were created for expression of Hprp3p or its mutants in bacterial or mammalian cells. We showed that antibodies against either Hprp3p or Hprp4p were able to pull-down the Hprp3p/Hprp4p complex formed in E. coli lysates. We demonstrated by co-immunoprecipitation and by isothermal titration calorimetry that purified Hprp3p and its mutants containing the central region, but lacking either the N-terminal 194 amino acids or the C-terminal 240 amino acids, were able to interact with Hprp4p. Conversely, Hprp3p-mutants containing only the N-terminal or C-terminal region did not interact with Hprp4p. In addition, we showed by co-immunoprecipitation that intact Hprp3p and its mutants containing the central region interact with Hprp4p in HeLa cell nuclear extracts. Primer extension analysis illustrated that the central region of Hprp3p is required to maintain the association of Hprp3p/Hprp4p with U4/U6 snRNAs, suggesting that this Hprp3p/Hprp4p interaction allows the recruitment of Hprp4p, and perhaps other protein(s), to the U4/U6 snRNP.
J. Biol. Chem, 10.1074/jbc.M111461200
Submitted on November 30, 2001
Revised on April 22, 2002
Accepted on April 22, 2002
Central region of the human splicing factor Hprp3p interacts with Hprp4p
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