Soullier S, Poulat F, Boizet-Bonhoure B, Calas B, Bennes R, Heitz F, Berta P
Centre de Recherche de Biochimie Macromoléculaire, CNRS UPR 9008/INSERM U249, Montpellier, France.
Biochimie. 1994;76(10-11):1075-81. doi: 10.1016/0300-9084(94)90033-7.
The product of the sex-determining gene SRY is a member of the HMG box containing protein superfamily. The HMG box is a DNA-binding domain of about 80 amino acids shared by many proteins with diverse functions. It seems that the functions of the full length protein are restricted to the HMG box but their molecular basis remains to be determined. We have summarized here the properties of this binding domain described so far in the literature and, using a synthetic peptide mimicking the DNA binding domain (SRY80), we have confirmed the existence of DNA minor groove contacts with this domain. Using intrinsic fluorescence of the tryptophane, the interaction between SRY80 and the putative target sequence AACAAAT was also quantified. In conclusion, we also consider the possible putative action of SRY to fulfill its role in sex determination.
