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The HMG box of SRY is a calmodulin binding domain
Author(s) -
Harley Vincent R.,
Lovell-Badge Robin,
Goodfellow Peter N.,
Hextall Patrick J.
Publication year - 1996
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 - 10.1016/0014-5793(96)00694-1
Subject(s) - testis determining factor , hmg box , calmodulin , binding site , dna binding domain , dna binding protein , electrophoretic mobility shift assay , binding domain , dna , transcription factor , biology , chemistry , microbiology and biotechnology , biochemistry , gene , y chromosome , enzyme
The HMG box domain of the testis determining factor, SRY, includes a basic amphiphilic sequence common to calmodulin (CaM) binding proteins. By affinity chromatography, native gel electrophoresis and fluorescence spectroscopy, we show the calcium‐dependent binding of SRY to CaM. Binding occurs via the HMG box and an SRY peptide of residues 57–80 binds CaM like the intact domain. SRY/CaM complex formation is specifically inhibited by the SRY DNA binding site sequence, AACAAT, but not a mutated sequence. Fluorescence spectra of the SRY/CaM complex indicate 1:1 stoichiometry and that binding is accompanied by a conformational change in SRY. The A domain of HMG1 also binds CaM and we propose that CaM binding is a property of the wider HMG box family, including SOX and TCF/LEF proteins. These results suggest that CaM may regulate the DNA binding activity of HMG box transcription factors.