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PMID: 1465398 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 24 ·1992-12-15 ·Pages 11779-83

Fisher DE, Parent LA, Sharp PA

Abstract

A distinct family of DNA-binding proteins is characterized by the presence of adjacent "basic," helix-loop-helix, and leucine zipper domains. Members of this family include the Myc oncoproteins, their binding partner Max, and the mammalian transcription factors USF, TFE3, and TFEB. Consistent with their homologous domains, these proteins bind to DNA containing the same core hexanucleotide sequence CACGTG. Analysis of the conformation of DNA in protein-DNA complexes has been undertaken with a circular permutation assay. Large mobility anomalies were detected for all basic/helix-loop-helix/leucine zipper proteins tested, suggesting that each protein induced a similar degree of bending. Phasing analysis revealed that basic/helix-loop-helix/leucine zipper proteins orient the DNA bend toward the minor groove. The presence of in-phase spacing between adjacent binding sites for this family of proteins in the immunoglobulin heavy-chain enhancer suggests the possible formation of an unusual triple-bended structure and may have implications for the activities of Myc.

MeSH Terms
Base Sequence Basic-Leucine Zipper Transcription Factors Binding Sites DNA/ultrastructure DNA-Binding Proteins/chemistry In Vitro Techniques Leucine Zippers Macromolecular Substances Molecular Sequence Data Nucleic Acid Conformation Oligodeoxyribonucleotides/chemistry Proto-Oncogene Proteins c-myc/chemistry Transcription Factors/chemistry
Chemicals
Basic-Leucine Zipper Transcription Factors DNA-Binding Proteins Macromolecular Substances Myc associated factor X Oligodeoxyribonucleotides Proto-Oncogene Proteins c-myc Transcription Factors DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fisher D E
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Parent L A
Sharp P A
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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.89.24.11779
Published
1992-12-15
Pages
11779-83
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC50640
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.89.24.11779 PMC Full Text View journal details
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