Chimeras of yeast and chicken calmodulin demonstrate differences in activation mechanisms of target enzymes

Biochemistry
K NakashimaM Yazawa

Abstract

Various chimeric proteins were constructed from yeast (Saccharomyces cerevisiae) and chicken calmodulin (CaM), and regions essential for target activation and responsible for the specific features of the yeast CaM were identified. The chimeric CaMs were designed so that each Ca2+ binding site of the yeast CaM was replaced in series from the C-terminus. Resulting CaM proteins showed Ca2+ binding properties inherent to the original Ca2+ binding site. Cooperative Ca2+ binding and a suitable rearrangement of the two EF-hand sites in each half-molecular domain were shown to be important for high-affinity interaction with CaM-dependent cyclic nucleotide phosphodiesterase (PDE). Residues in chicken CaM sequences 129-148 and 88-128, respectively, were required for low values of Kact (the concentration of CaM required for the half-maximal activation) in the activation of PDE and myosin light chain kinase (skMLCK and smMLCK). The difference in the structural requirements indicated different manners of the interaction. While PDE was activated to similar levels by different chimeras, the maximum activity (Vmax) given by chicken CaMs was not achieved by any chimeric CaMs in MLCKs. Residues in chicken CaM sequences 1-50 and 88-129, in additi...Continue Reading

Citations

Jun 7, 2014·Biochimica Et Biophysica Acta·Annegret Ulke-LeméeJustin A MacDonald
Oct 26, 1999·The Journal of Biological Chemistry·V S ReddyA S Reddy
Dec 13, 1996·The Journal of Biological Chemistry·A PersechiniI Ohashi
May 20, 2003·The Journal of Biological Chemistry·Laszlo FarkasLaszlo Nyitray

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