[HTML][HTML] Characterization of the threonine–phosphatase of mouse eyes absent 3
Eyes absent (EYA) has tyrosine-and threonine–phosphatase activities in their C-terminal
and N-terminal regions, respectively. Using various mutants of mouse EYA3, we showed
that the 68-amino acid domain between positions 53 and 120 was necessary and sufficient
for its threonine–phosphatase activity. Point mutations were then introduced, and residues
Cys-56, Tyr-77, His-79, and Tyr-90 were essential for the EYA3s threonine–phosphatase.
The 68-amino acid domain is not well conserved among the four mouse EYA members, but …
and N-terminal regions, respectively. Using various mutants of mouse EYA3, we showed
that the 68-amino acid domain between positions 53 and 120 was necessary and sufficient
for its threonine–phosphatase activity. Point mutations were then introduced, and residues
Cys-56, Tyr-77, His-79, and Tyr-90 were essential for the EYA3s threonine–phosphatase.
The 68-amino acid domain is not well conserved among the four mouse EYA members, but …
Eyes absent (EYA) has tyrosine- and threonine–phosphatase activities in their C-terminal and N-terminal regions, respectively. Using various mutants of mouse EYA3, we showed that the 68-amino acid domain between positions 53 and 120 was necessary and sufficient for its threonine–phosphatase activity. Point mutations were then introduced, and residues Cys-56, Tyr-77, His-79, and Tyr-90 were essential for the EYA3s threonine–phosphatase. The 68-amino acid domain is not well conserved among the four mouse EYA members, but is evolutionally highly conserved in the orthologous EYA members of different species, suggesting that the threonine–phosphatase of EYA3 has a function distinct from that of the other EYAs.
Elsevier