Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 25, Issue 8, Pages 2969-2980Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.25.8.2969-2980.2005
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- Medical Research Council [MC_U127584479] Funding Source: researchfish
- MRC [MC_U127584479] Funding Source: UKRI
- Medical Research Council [MC_U127584479] Funding Source: Medline
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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 U2AF(65)-related factor HCC1 as interacting proteins. In addition, SRrp53 is able to interact with some members of the SR family of proteins and with U2AF(35) 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.
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