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BioMetals : Volume 11, Issue 2, June 1998

BioMetals : Volume 11, Issue 1, March 1998

BioMetals : Volume 10

Metal ion binding to calmodulin: NMR and fluorescence studies

Content Provider	Springer Nature Link
Author	Ouyang, Hui Vogel, Hans J.
Copyright Year	1998
Abstract	Calmodulin is an important second messenger protein which is involved in a large variety of cellular path-ways.Calmodulin is sensitive to fluctuations in the intracellular Ca levels and is activated by the bindingof four Ca ions. In spite of the important role it plays in signal transduction pathways, it shows a surpris-inglybroad specificity for binding metal ions. Using 15N-Gly biosynthetically-labelled calmodulin, we havestudied the binding of different metal ions to calmodulin, including K+, Na+, Ca, Mg, Zn, Cd, Pb, Hg, Sr, La and Lu, by 1H, 15N HMQC NMR experiments. The effects of these ions on the substrate-bindingability of calmodulin have also been studied by fluorescence spectroscopy of the single tryptophan residue in a 22-residue synthetic peptide encompassing the skeletal muscle myosin light chain kinase calmod-ulin-binding domain. Most of these metal ions can activate a calmodulin target enzyme to some extent,though they bind to calmodulin in a different manner. Mg, which is of direct physiological interest, has adistinct site-preference for calmodulin, as it shows the highest affinity for site I in the N-terminal domain,while the C-terminal sites III and IV are the high affinity binding sites for Ca (as well as for Cd ). At ahigh concentration of Mg and a low concentration of Ca, calmodulin can bind Mg in its N-terminallobe while the C-terminal domain is occupied by Ca; this species could exist in resting cells in which the Mg level significantly exceeds that of Ca. Moreover, our data suggest that the toxicity of Pb-which,like Sr, binds with an equal and high affinity to all four sites-may be related to its capacity to tightlybind and improperly activate calmodulin.
Starting Page	213
Ending Page	222
Page Count	10
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	11
Issue Number	3
e-ISSN	15728773
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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