Open AccessDof DNA‐Binding Domains of Plant Transcription Factors Contribute to Multiple Protein‐Protein Interactions
Author(s) -
Yanagisawa Shuichi
Publication year - 1997
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1997.0403a.x
Subject(s) - homomeric , zinc finger , transcription factor , tbx1 , dna binding protein , transcription (linguistics) , hmg box , dna , high mobility group , biology , microbiology and biotechnology , dna binding domain , protein–protein interaction , protein domain , b3 domain , binding domain , chemistry , biochemistry , binding site , protein subunit , promoter , gene , gene expression , linguistics , philosophy
Dof proteins are a family of plant transcription factors that have a strongly conserved DNA‐binding domain, designated the Dof domain. This domain has the potential to form a single zinc finger. This report describes the self‐association of a maize Dof protein, Dof1 (previously designated MNB1a). Affinity chromatography revealed that Dof1 also interacted with another maize Dof protein, Dof2, as well as with high‐mobility‐group (HMG) protein 1. Results of mapping of the region required for the protein‐protein interactions of Dof1 suggested that these interactions may be mediated by the Dof domain. When gel mobility shift assays were performed with purified recombinant Dof proteins, homomeric and heteromeric complexes of Dof proteins on DNA were detected. It seems possible that formation of complexes of different Dof proteins through direct protein‐protein interactions might be involved in the regulation of transcription. Evidence is also presented that HMG1 has an effect on the binding of Dof1 to DNA. Therefore, it appears that the Dof domain is a multifunctional domain that is involved not merely in binding to DNA but also in multiple protein‐protein interactions.