We have studied the expression of the human SRY protein (termed p27SRY
) in two different cell lines by using specific antibodies. Confocal m
icroscopy enabled us to localize p27SRY precisely in the nucleus in a
discrete punctuate pattern. Furthermore, through microinjection experi
ments, we have demonstrated that the localization of the p27SRY protei
n into the nucleus was an event involving the NH2-terminal part of the
high mobility group (HMG) domain. With the help of several synthetic
peptides and various p27SRY mutants, we have characterized a bipartite
basic motif in this part of the protein corresponding to a nuclear lo
calization signal. This nuclear localization signal appears to be high
ly conserved in SRY box- and HMB box-containing proteins, suggesting c
ommon properties of nuclear targeting within the HMG box protein famil
y.