NGFIA (EGR1) contains transcription activating domains in both the amino terminal and carboxyl terminal region of the protein Academic Article uri icon

Overview

MeSH Major

  • DNA-Binding Proteins
  • Transcription Factors
  • Transcription, Genetic

abstract

  • We constructed and tested a number of lac repressor fusion proteins containing various portions of the zinc-finger containing protein NGFIA for their ability to stimulate transcription of a reporter gene containing lac operators. NGFIA contains two transcription activation regions, found in two distinct regions of the protein. The carboxyl (C) terminal portion of the molecule contains a weak activation domain, including five tandem copies of an eight amino acid repeat (T/S,T/S,F/Y,P,S,P,X,X). These five tandem copies of the repeated sequence activated reporter gene transcription 4-7 fold. Amino acids 1 through 293 in the amino (N) terminus of NGFIA function as a strong transcription activation domain stimulating transcription up to 80-fold. Fusions including amino acids 1-393 failed to activate transcription, indicating the presence of a domain capable of suppressing the N-terminal transcriptional activation function.

publication date

  • January 1993

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1993.1837

PubMed ID

  • 8392841

Additional Document Info

start page

  • 425

end page

  • 31

volume

  • 194

number

  • 1