Characterisation of tyrosine-phosphorylation-defective calmodulin mutants.

@article{Salas2005CharacterisationOT,
  title={Characterisation of tyrosine-phosphorylation-defective calmodulin mutants.},
  author={Valentina Salas and Juan S{\'a}nchez-Torres and David M Cusid{\'o}-Hita and Yael Garc{\'i}a-March{\'a}n and Felipe Sojo and Gustavo Benaim and Antonio Villalobo},
  journal={Protein expression and purification},
  year={2005},
  volume={41 2},
  pages={384-92}
}
Using site-directed mutagenesis, we have produced three calmodulin (CaM) mutants in which one or the two tyrosine residues of native CaM were substituted by phenylalanine. The three variants, denoted CaM(Y99F), CaM(Y138F), and CaM(Y99F/Y138F), were highly expressed in transformed Escherichia coli BL21(DE3)pLysS and purified in high yield. The three CaM mutants were able to activate the cyclic nucleotide phosphodiesterase and the plasma membrane Ca(2+)-ATPase, and present the characteristic Ca(2… CONTINUE READING