PMID: 8461293Apr 6, 1993Paper

Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae

Biochemistry
M A StarovasnikR E Klevit

Abstract

The Ca(2+)-binding and structural properties of calmodulin (CaM) from the yeast Saccharomyces cerevisiae (yCaM) were analyzed by flow dialysis and NMR spectroscopy. Full-length yCaM and two truncated versions of yCaM were expressed in Escherichia coli and purified. yTR1 (residues 1-76) and yTR2 (residues 75-147) are similar to the vertebrate CaM fragments TR1 and TR2, which are generated by limited proteolysis with trypsin. As was found for the fragments of vertebrate CaM, the yCaM fragments retain native conformation and are useful for examining structure and metal-binding properties by NMR. Evidence for a short beta-sheet in each domain, as well as characteristic NOEs to aromatic residues, suggests that yCaM folds similarly to vertebrate CaM. Furthermore, although the previously considered "invariant" glycine at position 6 is replaced by a histidine in site II of yCaM, the far downfield chemical shift of His-61's amide proton suggests that this site adopts a conformation similar to that found in other EF-hand sites. Macroscopic Ca(2+)-binding constants were determined for yCaM by flow dialysis, revealing three high-affinity sites (dissociation constants were 5.2, 3.3, and 2.3 microM in the presence of 1 mM MgCl2 and 100 mM KC...Continue Reading

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Citations

Aug 13, 2009·Journal of Mathematical Biology·Fusheng Tang, Weijiu Liu
May 24, 2003·Journal of Inorganic Biochemistry·Bodil W Rasmussen, Morten J Bjerrum
Nov 3, 2006·Molecular Biology of the Cell·Andreas UttenweilerAndreas Mayer
Feb 18, 2016·Proceedings of the National Academy of Sciences of the United States of America·D Brent HallingRichard W Aldrich
Mar 29, 2005·Biophysical Chemistry·Kenosha F HobsonSusan Pedigo
Aug 18, 2017·Molecular Biology of the Cell·Shruthi ViswanathEric G Muller
Aug 2, 2005·The Journal of Biological Chemistry·Andreas UttenweilerAndreas Mayer
Jul 3, 1999·Physiological Reviews·L A JuradoH W Jarrett

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