Oncogenic EWS-Fli1 interacts with hsRPB7, a subunit of human RNA polymerase II View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-08-06

AUTHORS

Robert Petermann, Birgit M Mossier, Dave NT Aryee, Vladimir Khazak, Erica A Golemis, Heinrich Kovar

ABSTRACT

As a result of the t(11;22)(q24;q12) chromosomal translocation characterizing the Ewing family of tumors (ET), the amino terminal portion of EWS, an RNA binding protein of unknown function, is fused to the DNA-binding domain of the ets transcription factor Fli1. The hybrid EWS-Fli1 protein acts as a strong transcriptional activator and, in contrast to wildtype Fli1, is a potent transforming agent. Similar rearrangements involving EWS or the highly homologous TLS with various transcription factors have been found in several types of human tumors. Employing yeast two-hybrid cloning we isolated the seventh largest subunit of human RNA polymerase II (hsRPB7) as a protein that specifically interacts with the amino terminus of EWS. This association was confirmed by in vitro immunocoprecipitation. In nuclear extracts, hsRPB7 was found to copurify with EWS-Fli1 but not with Fli1. Overexpression of recombinant hsRPB7 specifically increased gene activation by EWS-chimeric transcription factors. Replacement of the EWS portion by hsRPB7 in the oncogenic fusion protein restored the transactivating potential of the chimera. Our results suggest that the interaction of the amino terminus of EWS with hsRPB7 contributes to the transactivation function of EWS-Fli1 and, since hsRPB7 has characteristics of a regulatory subunit of RNA polymerase II, may influence promoter selectivity. More... »

PAGES

603-610

Journal

TITLE

Oncogene

ISSUE

5

VOLUME

17

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1201964

DOI

http://dx.doi.org/10.1038/sj.onc.1201964

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005008704

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9704926


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