ZNF265 - A novel spliceosomal protein able to induce alternative splicing

David J. Adams, Louise Van Der Weyden, Akila Mayeda, Stefan Stamm, Brian J. Morris, John E.J. Rasko

Research output: Contribution to journalArticlepeer-review

64 Scopus citations


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-β1 transcripts in a dose-dependent manner in HEK 293 cells. Yeast two-hybrid analysis and immunoprecipitation indicated interaction of ZNF265 with the essential splicing factor proteins U1-70K and U2AF35. 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.

Original languageEnglish
Pages (from-to)25-32
Number of pages8
JournalJournal of Cell Biology
Issue number1
StatePublished - Jul 9 2001


  • Nuclear localization
  • RNA processing
  • RS domain
  • Renin
  • SR proteins
  • Zinc finger protein

ASJC Scopus subject areas

  • Cell Biology


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