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The GCM domain is a Zn‐coordinating DNA‐binding domain
Author(s) -
Cohen Serge X,
Moulin Martine,
Schilling Oliver,
Meyer-Klaucke Wolfram,
Schreiber Jörg,
Wegner Michael,
Müller Christoph W
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03257-x
Subject(s) - gcm transcription factors , cysteine , domain (mathematical analysis) , dna , histidine , chemistry , dna binding domain , sequence (biology) , binding domain , binding site , crystallography , biophysics , biochemistry , amino acid , biology , gene , transcription factor , general circulation model , ecology , mathematical analysis , mathematics , climate change , enzyme
Glial cells missing (GCM) proteins form a small family of transcriptional regulators involved in different developmental processes. They contain a DNA‐binding domain that is highly conserved from flies to mice and humans and consists of approximately 150 residues. The GCM domain of the mouse GCM homolog a was expressed in bacteria. Extended X‐ray absorption fine structure and particle‐induced X‐ray emission analysis techniques showed the presence of two Zn atoms with four‐fold coordination and cysteine/histidine residues as ligands. Zn atoms can be removed from the GCM domain by the Zn chelator phenanthroline only under denaturating conditions. This suggests that the Zn ions are buried in the interior of the GCM domain and that their removal abolishes DNA‐binding because it impairs the structure of the GCM domain. Our results define the GCM domain as a new type of Zn‐coordinating, sequence‐specific DNA‐binding domain.