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09:51
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
DNA sequence-dependent folding determines the divergence in binding specificities between Maf and other bZIP proteins
M Dlakić1, A V Grinberg, D A Leonard
1Howard Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0650, USA.
The EMBO Journal
|February 17, 2001
Summary
Maf proteins, a type of transcription factor, uniquely bind DNA through a conformational change. This allows them to recognize extended DNA elements, unlike other bZIP proteins.
Area of Science:
- Molecular Biology
- Protein-DNA Interactions
Background:
- Maf proteins are atypical basic region-leucine zipper (bZIP) transcription factors.
- They possess a variant basic region and an ancillary DNA-binding region, enabling recognition of extended DNA elements beyond canonical bZIP binding sites.
Purpose of the Study:
- To elucidate the molecular mechanisms underlying the distinct DNA recognition specificity of Maf proteins compared to other bZIP family members.
- To investigate the structural and functional basis for Maf's ability to bind extended DNA sequences.
Main Methods:
- Analysis of Maf protein secondary structure and trypsin sensitivity.
- Measurement of DNA binding affinity and dissociation rates.
- Determination of nucleotide base contacts made by Maf proteins.
Main Results:
- Maf DNA binding is intrinsically linked to a conformational change in its basic and ancillary DNA-binding regions, triggered by extended DNA elements.
- Specific amino acid differences in the Maf basic region facilitate this conformational change.
- Maf proteins exhibit distinct nucleotide base contact patterns compared to canonical bZIP proteins.
Conclusions:
- The unusual DNA binding specificity of Maf proteins arises from the coordinated folding of distinct DNA recognition motifs.
- Conformational flexibility and unique amino acid residues are key to Maf's recognition of extended DNA elements.
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