Abstract
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.
Publication types
-
Case Reports
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adolescent
-
Amenorrhea / genetics*
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
DNA / blood
-
DNA / isolation & purification
-
DNA Primers
-
DNA-Binding Proteins / genetics*
-
Female
-
Humans
-
Leukocytes / metabolism
-
Molecular Sequence Data
-
Nuclear Proteins*
-
Point Mutation*
-
Polymerase Chain Reaction
-
Sequence Homology, Amino Acid
-
Sex Determination Analysis*
-
Sex-Determining Region Y Protein
-
Transcription Factors / genetics
-
X Chromosome
-
Y Chromosome
Substances
-
DNA Primers
-
DNA-Binding Proteins
-
Nuclear Proteins
-
SRY protein, human
-
Sex-Determining Region Y Protein
-
Transcription Factors
-
DNA