1. ZNF265--a novel spliceosomal protein able to induce alternative splicing
- Author
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Adams, David J., van der Weyden, Louise, Mayeda, Akila, Stamm, Stefan, Morris, Brian J., and Rasko, John E.J.
- Subjects
Cell research -- Analysis ,RNA splicing -- Physiological aspects ,Biological sciences - Abstract
The formation of the active spliceosome, its recruitment to active areas of transcription, and its role in pre-mRNA splicing depends on the association of a number of multifunctional serine/arginine-rich (SR) proteins. ZNF265 is an arginine/serine-rich (RS) domain containing zinc finger protein with conserved pre-mRNA splicing protein motifs. Here we show that ZNF265 immunoprecipitates from splicing extracts in association with mRNA, and that it is able to alter splicing patterns of Tra2-[Beta]1 transcripts in a dose-dependent manner in HEK 293 cells. Yeast two-hybrid analysis and immunoprecipitation indicated inter action of ZNF265 with the essential splicing factor proteins U1-70K and [U2AF.sup.35]. Confocal microscopy demonstrated colocalization of ZNF265 with the motor neuron gene product SMN, the snRNP protein U1-70K, the SR protein SC35, and with the transcriptosomal components p300 and YY1. Transfection of HT-1080 cells with ZNF265-EGFP fusion constructs showed that nuclear localization of ZNF265 required the RS domain. Alignment with other RS domain-containing proteins revealed a high degree of SR dipeptide conservation. These data show that ZNF265 functions as a novel component of the mRNA processing machinery.
- Published
- 2001