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 o
f 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 min
or groove contacts with this domain. Using intrinsic fluorescence of t
he 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 fullfil its role in sex determi
nation.