A novel SR-related protein is required for the second step of Pre-mRNA splicing.
The SR family proteins and SR-related polypeptides are important regulators of pre-mRNA splicing. A novel SR-related protein of an apparent molecular mass of 53 kDa was isolated in a gene trap screen that identifies proteins which localize to the nuclear speckles. This novel protein possesses an arginine- and serine-rich domain ... and was termed SRrp53 (for SR-related protein of 53 kDa). In support for a role of this novel RS-containing protein in pre-mRNA splicing, we identified the mouse ortholog of the Saccharomyces cerevisiae U1 snRNP-specific protein Luc7p and the U2AF65-related factor HCC1 as interacting proteins. In addition, SRrp53 is able to interact with some members of the SR family of proteins and with U2AF35 in a yeast two-hybrid system and in cell extracts. We show that in HeLa nuclear extracts immunodepleted of SRrp53, the second step of pre-mRNA splicing is blocked, and recombinant SRrp53 is able to restore splicing activity. SRrp53 also regulates alternative splicing in a concentration-dependent manner. Taken together, these results suggest that SRrp53 is a novel SR-related protein that has a role both in constitutive and in alternative splicing.
Mesh Terms:
Alternative Splicing, Amino Acid Sequence, Animals, Cell Nucleus, Cloning, Molecular, Cytoplasm, Hela Cells, Humans, Mice, Molecular Sequence Data, Nuclear Proteins, RNA Precursors, RNA Splice Sites, RNA, Messenger, RNA-Binding Proteins, Sequence Homology, Amino Acid, Two-Hybrid System Techniques
Alternative Splicing, Amino Acid Sequence, Animals, Cell Nucleus, Cloning, Molecular, Cytoplasm, Hela Cells, Humans, Mice, Molecular Sequence Data, Nuclear Proteins, RNA Precursors, RNA Splice Sites, RNA, Messenger, RNA-Binding Proteins, Sequence Homology, Amino Acid, Two-Hybrid System Techniques
Mol. Cell. Biol.
Date: Apr. 01, 2005
PubMed ID: 15798186
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