NGFIA (EGR1) Contains Transcription Activating Domains in Both the Amino Terminal and Carboxyl Terminal Regions of the Protein

Christopher Defranco, Marguerite Ro, Martha Grossel, Milton A. English, Ulla M. Hansen, John A. Wagner, Jonathan D. Licht

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

We constructed and tested a number of lac repressor fusion proteins containing various portions of the zinc-finger conatining 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 though 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 adomain capable of supressing the N-terminal transcriptional activation function.

Original languageEnglish
Pages (from-to)425-431
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume194
Issue number1
DOIs
StatePublished - 15 Jul 1993

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