Poulat F, Soullier S, Gozé C, Heitz F, Calas B, Berta P
Centre de Recherche de Biochimie Macromoléculaire, CNRS UPR 9008, INSERM U. 249, Montpellier, France.
Hum Mutat. 1994;3(3):200-4. doi: 10.1002/humu.1380030305.
The sex-determining gene SRY was screened for molecular alteration in an XY sex-reversed female by single-strand conformation polymorphism (SSCP) technique. An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. The affected tyrosine residue located at the C terminus of the DNA binding protein is evolutionarily strongly conserved among the members of the HMG box containing proteins. Using gel shift assay and peptide synthesis such a mutation is shown to abolish the SRY protein DNA binding ability. The involvement of this particular amino acid in the binding specificity is also discussed.
