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J Biol Chem, Vol. 273, Issue 32, 20629-20635, August 7, 1998
From the Departments of Critical protein-protein interactions among
pre-mRNA splicing factors determine splicing efficiency and
specificity. The serine/arginine proteins, a family of factors
characterized by the presence of an RNA recognition motif and an
arginine/serine domain, are essential for constitutive splicing and
required for some alternative splicing decisions. ASF/SF2, SC35, and
other members of the serine/arginine family, interact with the 70k
protein of the U1 small nuclear ribonucleoprotein. The binding of this
protein with ASF/SF2 is thought to enhance recognition of the 5' splice
site of pre-mRNAs by the U1 small nuclear ribonucleoprotein. It has
been clearly documented that the arginine/serine domain of ASF/SF2 is
responsible for binding to the U1 70k protein. In this manuscript we
characterize the segment in the human U1 70k protein that is both
necessary and sufficient for ASF/SF2 binding. A domain within this
segment, which begins with Arg240 and ends with
Asp270, was shown to bind specifically to the
arginine/serine domain of ASF/SF2 using a yeast two-hybrid system and a
far Western assay. Mutational analysis of this segment suggested that
several arginines are critical for the interaction with ASF/SF2 and for
phosphorylation by SRPK1. Inspection of the sequence of the
Arg248 to Asp270 region suggested this as an
arginine/serine-like domain in U1 70k protein, and the data presented
in this manuscript strongly support this view. Inspection of the human
U1 70k protein sequence, comparison with homologues in other animal
species, and mutational analysis indicated the importance of the
sequence Arg-Arg-Arg-Ser-Arg-Ser-Arg-Asp, which is found repeated twice
in the region from Arg248 to Asp270 in the
human protein.
A Serine/Arginine-rich Domain in the Human U1 70k Protein Is
Necessary and Sufficient for ASF/SF2 Binding
and§¶
Pharmacology and Cancer
Biology, § Microbiology, and ¶ Medicine, Levine Science
Research Center, Duke University Medical Center,
Durham, North Carolina 27710
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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