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PMID: 8446581 Published · ppublish English Journal Article

A small single-"finger" peptide from the erythroid transcription factor GATA-1 binds specifically to DNA as a zinc or iron complex.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 5 ·1993-03-01 ·Pages 1676-80

Omichinski JG, Trainor C, Evans T, Gronenborn AM, Clore GM, Felsenfeld G

Abstract

Sequence-specific DNA binding has been demonstrated for a synthetic peptide comprising only one of the two "finger"-like domains of the erythroid transcription factor GATA-1 (also termed Eryf-1, NF-E1, or GF-1). Quantitative analysis of gel-retardation assays yields a specific association constant of 1.2 x 10(8) M, compared with values of about 10(9) M for the full-length natural GATA-1 protein. By the use of peptides of various lengths, it was possible to delineate the smallest region necessary for specific binding. A single C-terminal finger of the double-finger motif is necessary but not sufficient for sequence-specific interaction. Basic amino acids located C-terminal to the finger (some more than 20 amino acids away) are also essential for tight binding. In addition to demonstrating that zinc is important for the formation of an active binding complex, we show that other ions, notably Fe2+, can fulfill this role. Our results make it clear that the GATA-1 metal binding motif is quite distinct from that found in the steroid hormone family and that GATA-1 is a member of a separate class of DNA binding proteins.

Related Genes
Eryf1
MeSH Terms
Amino Acid Sequence Animals Base Sequence Chickens DNA/metabolism DNA-Binding Proteins/chemistry,metabolism Erythroid-Specific DNA-Binding Factors In Vitro Techniques Iron/chemistry Molecular Sequence Data Oligodeoxyribonucleotides/chemistry Peptides/chemistry,metabolism Transcription Factors/chemistry,metabolism Zinc/chemistry Zinc Fingers
Chemicals
DNA-Binding Proteins Erythroid-Specific DNA-Binding Factors Oligodeoxyribonucleotides Peptides Transcription Factors DNA Iron Zinc
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Omichinski J G
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Trainor C
Evans T
Gronenborn A M
Clore G M
Felsenfeld G
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.5.1676
Published
1993-03-01
Pages
1676-80
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC45942
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.90.5.1676 PMC Full Text View journal details
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