Activation of transcription by PU.1 requires both acidic and glutamine domains

Michael J. Klemsz, Richard A. Maki

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Abstract

The B-lymphocyte- and macrophage-specific transcription factor PU.1 is a member of the ets family of proteins. To understand how PU.1 functions as a transcription factor, we initiated a series of experiments to define its activation domain. Using deletion analysis, we showed that the activation domain of PU.1 is located in the amino-terminal half of the protein. Within this region, we identified three acidic subdomains and one glutamine-rich subdomain. The deletion of any of these subdomains resulted in a significant loss in the ability of PU.1 to transactivate in cotransfection studies. Amino acid substitution analysis showed that the activation of transcription by PU.1 requires acidic residues between amino acids 7 and 74 and a group of glutamine residues between amino acids 75 and 84. These data show that PU.1 contains two types of known activation domains and that both are required for maximal transactivation.

Original languageEnglish (US)
Pages (from-to)390-397
Number of pages8
JournalMolecular and cellular biology
Volume16
Issue number1
DOIs
StatePublished - Jan 1996

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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