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PMID: 11179227 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

DNA sequence-dependent folding determines the divergence in binding specificities between Maf and other bZIP proteins.

The EMBO journal ·Vol. 20 ·No. 4 ·2001-02-15 ·Pages 828-40

Dlakić M, Grinberg AV, Leonard DA, Kerppola TK

Abstract

Maf family transcription factors are atypical basic region-leucine zipper (bZIP) proteins that contain a variant basic region and an ancillary DNA-binding region. These proteins recognize extended DNA sequence elements flanking the core recognition element bound by canonical bZIP proteins. We have investigated the causes for the differences in DNA recognition between Maf and other bZIP family proteins through studies of Maf secondary structure, trypsin sensitivity, binding affinity, dissociation rate and DNA contacts. Our results show that specific DNA binding by Maf is coupled to a conformational change involving both the basic and ancillary DNA-binding regions that depends on the extended DNA sequence elements. Two basic region amino acid residues that differ between Maf and canonical bZIP proteins facilitate the conformational change required for Maf recognition of the extended elements. Nucleotide base contacts made by Maf differ from those made by canonical bZIP proteins. Taken together, our results suggest that the unusual DNA binding specificity of Maf family proteins is mediated by concerted folding of structurally unrelated DNA recognition motifs.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry,metabolism Base Sequence Basic-Leucine Zipper Transcription Factors Binding Sites DNA/metabolism DNA Footprinting DNA-Binding Proteins/chemistry,metabolism G-Box Binding Factors Molecular Sequence Data Oligodeoxyribonucleotides Protein Conformation Protein Folding Sequence Homology, Amino Acid Transcription Factors/chemistry,metabolism
Chemicals
Bacterial Proteins Basic-Leucine Zipper Transcription Factors DNA-Binding Proteins G-Box Binding Factors Maf protein, Bacillus subtilis Oligodeoxyribonucleotides Transcription Factors DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dlakić M
Howard Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0650, USA.
Grinberg A V
Leonard D A
Kerppola T K
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/20.4.828
Published
2001-02-15
Pages
828-40
Language
English
Region
England
NLM ID
8208664
PMCID
PMC145405
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/20.4.828 PMC Full Text View journal details
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