Transcriptional activation by ETS and leucine zipper-containing basic helix-loop-helix proteins

Gang Tian, Batu Erman, Haruhiko Ishii, Samudra S. Gangopadhyay, Ranjan Sen

Research output: Contribution to journalArticlepeer-review

Abstract

The immunoglobulin μ heavy-chain gene enhancer contains closely juxtaposed binding sites for ETS and leucine zipper-containing basic helix- loop-helix (bHLH-zip) proteins. To understand the μ enhancer function, we have investigated transcription activation by the combination of ETS and bHLH-zip proteins. The bHLH-zip protein TFE3, but not USF, cooperated with the ETS domain proteins PU.1 and Ets-1 to activate a tripartite domain of this enhancer. Deletion mutants were used to identify the domains of the proteins involved. Both TFE3 and USF enhanced Ets-1 DNA binding in vitro by relieving the influence of an autoinhibitory domain in Ets-1 by direct protein-protein associations. Several regions of Ets-1 were found to be necessary, whereas the bHLH-zip domain was sufficient for this effect. Our studies define novel interactions between ETS and bHLH-zip proteins that may regulate combinatorial transcription activation by these protein families.

Original languageEnglish (US)
Pages (from-to)2946-2957
Number of pages12
JournalMolecular and Cellular Biology
Volume19
Issue number4
StatePublished - Apr 1999
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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