Identification of a novel transcriptional activity of mammalian Id proteins

Mangkey A. Bounpheng, Irena N. Melnikova, Joseph J. Dimas, Barbara A. Christy

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

The Id proteins are a family of related mammalian helix-loop-helix (HLH) proteins which can interact with other HLH proteins but lack a basic region and are thus not thought to bind to DNA. Instead, they are hypothesized to act as dominant negative regulators of DNA-binding basic HLH (bHLH) proteins, by forming inactive heterodimers with these proteins. All four Id family proteins possess related HLH dimerization domains and can interact with similar bHLH proteins, although with differing affinities. The functions of the largely unrelated N- and C-terminal regions of the proteins are unknown. In this study, we have identified a novel transcriptional activity of the mammalian Id proteins. We show that when fused to the heterologous GAL4 DNA-binding domain, all four of the mammalian Id proteins can activate GAL4-dependent transcription. The HLH domain is necessary for the transactivation activity observed, suggesting that interaction with a cellular HLH protein is required. Co-transfection with exogenous Class A bHLH proteins (E-proteins) greatly potentiates the transactivation, which is abolished upon co-transfection with Class B bHLH proteins. These results are consistent with the idea that the Id proteins have a transcriptional activity when present in a DNA-binding complex.

Original languageEnglish (US)
Pages (from-to)1740-1746
Number of pages7
JournalNucleic acids research
Volume27
Issue number7
DOIs
StatePublished - Apr 1 1999

ASJC Scopus subject areas

  • Genetics

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