FEBS Letters | |
The HMG box of SRY is a calmodulin binding domain | |
Hextall, Patrick J.1  Harley, Vincent R.1  Goodfellow, Peter N.1  Lovell-Badge, Robin2  | |
[1] Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK;MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK | |
关键词: HMG box; SRY; Calmodulin; DNA binding; | |
DOI : 10.1016/0014-5793(96)00694-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020303039ZK.pdf | 625KB | download |