Unknown

Dataset Information

0

ZNF265--a novel spliceosomal protein able to induce alternative splicing.


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-beta1 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 U2AF(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.

SUBMITTER: Adams DJ 

PROVIDER: S-EPMC2196870 | biostudies-literature | 2001 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

ZNF265--a novel spliceosomal protein able to induce alternative splicing.

Adams D J DJ   van der Weyden L L   Mayeda A A   Stamm S S   Morris B J BJ   Rasko J E JE  

The Journal of cell biology 20010701 1


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-beta1 t  ...[more]

Similar Datasets

| S-EPMC3042160 | biostudies-literature
| S-EPMC5829640 | biostudies-literature
| S-EPMC3113647 | biostudies-literature
| S-EPMC6283158 | biostudies-literature
2011-02-01 | E-GEOD-26463 | biostudies-arrayexpress
| S-EPMC2447145 | biostudies-literature
| S-EPMC316838 | biostudies-literature
2011-02-01 | GSE26463 | GEO
| S-EPMC6805012 | biostudies-literature
| S-EPMC8040622 | biostudies-literature