ArticleThe EMBO journal2001
DNA sequence-dependent folding determines the divergence in binding specificities between Maf and other bZIP proteins.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Review
- MAFB: a key regulator of myeloid commitment involved in hematological diseases.Cell death discovery · 2025Review
- The role and regulation of Maf proteins in cancer.Biomarker research · 2023Review
- Loss of Mafb and Maf distorts myeloid cell ratios and disrupts fetal mouse testis vascularization and organogenesis†.Biology of reproduction · 2021Article
- The ancillary N-terminal region of the yeast AP-1 transcription factor Yap8 contributes to its DNA binding specificity.Nucleic acids research · 2020Article
- Identification of specific DNA binding residues in the TCP family of transcription factors in Arabidopsis.The Plant cell · 2010Article
- Structural basis of alternative DNA recognition by Maf transcription factors.Molecular and cellular biology · 2009Article
- The transcription factor Lc-Maf participates in Col27a1 regulation during chondrocyte maturation.Experimental cell research · 2009Article
- Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions.The Journal of biological chemistry · 2008Article
- CD13/APN transcription is regulated by the proto-oncogene c-Maf via an atypical response element.Gene · 2007Article
- Expression, purification, crystallization and preliminary crystallographic analysis of the mouse transcription factor MafB in complex with its DNA-recognition motif Cmare.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Article
- Large Maf Transcription Factors: Cousins of AP-1 Proteins and Important Regulators of Cellular Differentiation.The Einstein journal of biology and medicine : EJBM · 2007Article
- Combinatorial control of Arabidopsis proline dehydrogenase transcription by specific heterodimerisation of bZIP transcription factors.The EMBO journal · 2006Article
- Regulation of insulin gene expression by overlapping DNA-binding elements.The Biochemical journal · 2005Article
- The 5'-AT-rich half-site of Maf recognition element: a functional target for bZIP transcription factor Maf.Nucleic acids research · 2005Article
- c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK).Oncogene · 2004Article
- Synergistic transcription activation by Maf and Sox and their subnuclear localization are disrupted by a mutation in Maf that causes cataract.Molecular and cellular biology · 2004Article
- Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1.Molecular and cellular biology · 2003Article
- Classification of human B-ZIP proteins based on dimerization properties.Molecular and cellular biology · 2002Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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