Solution structure of the DNA-binding domain of MafG

Hideki Kusunoki, Hozumi Motohashi, Fumiki Katsuoka, Akio Morohashi, Masayuki Yamamoto, Toshiyuki Tanaka

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the DNA-binding domain (residues 1-76) of MafG, which contains the EHR and the basic region. The structure consists of three α-helices and resembles the fold of the DNA-binding domain of Skn-1, a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins recognize their consensus DNA sequences.

Original languageEnglish
Pages (from-to)252-256
Number of pages5
JournalNature Structural Biology
Volume9
Issue number4
DOIs
Publication statusPublished - 2002 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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