Identification of ERF-1 as a member of the AP2 transcription factor family

Lisa A McPherson; Vijay R Baichwal; Ronald J Weigel

doi:10.1073/pnas.94.9.4342

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Identification of ERF-1 as a member of the AP2 transcription factor family

Journal article

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Identification of ERF-1 as a member of the AP2 transcription factor family

Lisa A McPherson, Vijay R Baichwal and Ronald J Weigel

Proceedings of the National Academy of Sciences - PNAS, Vol.94(9), pp.4342-4347

04/29/1997

DOI: 10.1073/pnas.94.9.4342

PMCID: PMC20724

PMID: 9113991

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Abstract

The ERF-1 transcription factor was previously shown to be involved in the regulation of estrogen receptor (ER) gene transcription in hormonally responsive breast and endometrial carcinomas. In this study we sought to identify the gene for ERF-1. ERF-1 activates ER gene transcription by binding to the imperfect palindrome CCCTGCGGGG within the promoter of the ER gene. ERF-1 protein was purified from the ER-positive breast carcinoma cell line, MCF7, utilizing ion exchange and DNA affinity chromatography. Peptide sequence analysis was used to isolate a 2.7 kb cDNA clone from an MCF7 cDNA library. This cDNA encodes a protein of 48 kDa previously identified as the AP2γ transcription factor. By gel-shift analysis, in vitro synthesized ERF-1 comigrates with MCF7 native ERF-1 complex and demonstrates identical sequence binding specificity as native ERF-1. In addition, AP2 polyclonal antisera supershifts both in vitro synthesized and native ERF-1 complexes. These results show that ERF-1 is a member of the AP2 family of developmentally regulated transcription factors. Given the central role of ER expression in breast carcinoma biology, ERF-1 is likely to regulate expression of a set of genes characteristic of the hormonally-responsive breast cancer phenotype.

Biological Sciences

Breast Cancer

RNA

promoter

estrogen receptor

gene

Details

Title: Subtitle: Identification of ERF-1 as a member of the AP2 transcription factor family
Creators: Lisa A McPherson - Department of Surgery, Stanford University, Stanford, CA 94305; and
Vijay R Baichwal - Department of Surgery, Stanford University, Stanford, CA 94305; and
Ronald J Weigel - Department of Surgery, Stanford University, Stanford, CA 94305; and
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.94(9), pp.4342-4347
DOI: 10.1073/pnas.94.9.4342
PMID: 9113991
PMCID: PMC20724
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences
Language: English
Date published: 04/29/1997
Academic Unit: Molecular Physiology and Biophysics; Anatomy and Cell Biology; Surgery; Biochemistry and Molecular Biology
Record Identifier: 9984025254702771

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