Biochemical properties of V91G calmodulin: A calmodulin point mutation that deregulates muscle contraction in Drosophila

Protein Science

Volumn 13, Issue 12, 2004, Pages 3285-3297

  Wang, Bo ^a,e   Martin, Stephen R ^b   Newman, Rhonda A ^c   Hamilton, Susan L ^d   Shea, Madeline A ^c   Bayley, Peter M ^b   Beckingham, Kathleen M ^a  

^a RICE UNIVERSITY   (United States)

^b NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^c UNIVERSITY OF IOWA   (United States)

^d BAYLOR COLLEGE OF MEDICINE   (United States)

^e Union Biometrica   (United States)

Author keywords

Calcium channels; Calcium signaling in Drosophila; Calmodulin mutant phenotype; Ryanodine receptor

Indexed keywords

CALCIUM CHANNEL; CALMODULIN; MUTANT PROTEIN; RYANODINE RECEPTOR;

AMINO ACID SUBSTITUTION; ARTICLE; CALCIUM BINDING; CALCIUM SIGNALING; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; DROSOPHILA; FLUORESCENCE; GEL ELECTROPHORESIS; HYDROPHOBICITY; MUSCLE CONTRACTION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STOICHIOMETRY; WILD TYPE;

ANIMALS; BINDING SITES; CALCIUM; CALMODULIN; DROSOPHILA; DROSOPHILA PROTEINS; MUSCLE CONTRACTION; MUSCLES; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL;

MAMMALIA;

EID: 9344222212     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04928204     Document Type: Article

References (45)

1. Bayley, P.M., Findlay, W.A., and Martin, S.R. 1996. Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Sci. 5: 1215-1228.
2. 2(+)- induced conformational changes. J. Biol. Chem. 266: 6027-6030.
3. Clapham, D.E. 1995. Calcium signaling. Cell 80: 259-268.
4. Cohen, P. and Klee, C.B. 1988. Calmodulin: Molecular aspects of cellular regulation. Elsevier Press, New York.
5. Cyert, M.S. 2001. Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Anna. Rev. Genet. 35: 647-672.
6. Finn, B.E., Drakenberg, T., and Forsen, S. 1993. The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain. FEBS Lett. 336: 368-374.
7. GuptaRoy, B., Marwaha, N., Pla, M., Wang, Z., Nelson, H.B., Beckingham, K., and Griffith, L.C. 2000. Alternative splicing of Drosophila calcium/calmodulin-dependent protein kinase II regulates substrate specificity and activation. Brain Res. Mol. Brain Res. 80: 26-34.
8. 2+ binding sites of calmodulin. J. Biol. Chem. 271: 761-767.
9. Keller, C.H., Olwin, B.B., LaPorte, D.C., and Storm, D.R. 1982. Determination of the free-energy coupling for binding of calcium ions and troponin 1 to calmodulin. Biochemistry 21: 156-162.
10. Kojima, S., Mishima, M., Mabuchi, I., and Hotta, Y. 1996. A single Drosophila melanogaster myosin light chain kinase gene produces multiple isoforms whose activities are differently regulated. Genes Cells 1: 855-871.
11. (2+)-dependent conformational change of calmodulin. FEBS Lett. 521: 133-139.
12. Kuboniwa, H., Tjandra, N., Grzesiek, S., Ren, H., Klee, C.B., and Bax, A. 1995. Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2: 768-776.
13. Laporte, D.C., Wierman, B.M., and Storm, D.R. 1980. Calcium-induced exposure of a hydrophobic surface on calmodulin. Biochemistry 19: 3814-3819.
14. 2(+)-ATPase of Drosophila melanogaster. Biochem. Biophy. Res. Commun. 173: 872-877.
15. Martin, S.R. and Bayley, P.M. 2002. Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin, V. Protein Sci. 11: 2909-2923.
16. Martin, S.R., Bayley, P.M., Brown, S.E., Porumb, T., Zhang, M., and Ikura, M. 1996. Spectroscopic characterization of a high-affinity calmodulin-target peptide hybrid molecule. Biochemistry 35: 3508-3517.
17. Masino, L., Martin, S.R., and Bayley, P.M. 2000. Ligand binding and thermodynamic stability of a multidomain protein, calmodulin. Protein Sci. 9: 1519-1529.
18. 2+)-binding sites of calmodulin. J. Biol. Chem. 267: 5286-5295.
19. 2+ binding site mutants of Drosophila melanogaster calmodulin. Biochemistry 31: 7779-7786.
20. Mukherjea, P., Maune, J.F., and Beckingham, K. 1996. Interlobe communication in multiple calcium-binding site mutants of Drosophila calmodulin. Protein Sci. 5: 468-477.
21. Nelson, H.B., Heiman, R.G., Bolduc, C., Kovalick, G.E., Whitley, P., Stern, M., and Beckingham, K. 1997. Calmodulin point mutations affect Drosophila development and behavior. Genetics 147: 1783-1798.
22. 2+-dependent inactivation of L-type calcium channels. Neuron 22: 549-558.
23. Putney Jr., J.W. 1998. Calcium signaling: Up, down, up, down, what's the point? Science 279: 191-192.
24. 2+) and calmodulin. Biochemistry 39: 7807-7812.
25. Rodney, G.G., Moore. C.P., Williams, B.Y., Zhang, J.Z., Krol, J., Pedersen, S.E., and Hamilton, S.L. 2001a. Calcium binding to calmodulin leads to an N-terminal shift in its binding site on the ryanodine receptor J. Biol. Chem. 276: 2069-2074.
26. Rodney, G.G., Krol, J., Williams, B., Beckingham, K., and Hamilton, S.L. 2001b. The carboxy-terminal calcium binding sites of calmodulin control calmodulin's switch from an activator to an inhibitor of RYR1. Biochemistry 40: 12430-12435.
27. Saimi, Y. and Kung, C. 2002. Calmodulin as an ion channel subunit. Ann. Rev. Physiol. 64: 289-311.
28. Schulman, H. and Braun, A. 1999. Calcium/calmodulin dependent kinases. In Calcium as cellular regulator (eds. E. Carafoli and C. Klee), pp. 311-343. Oxford University Press. Oxford.
29. (2+)-transporting ATPase from the sarcoplasmic reticulum of the cross-striated part of the adductor muscle of the deep sea scallop: Comparison to serca enzymes of other animals. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 120: 359-374.
30. Sobolev, V., Sorokine, A., Prilusky, J., Abola, E.E., and Edelman, M. 1999. Automated analysis of interatomic contacts in proteins. Bioinformatics 15: 327-332.
31. Takeshima, H., Nishi, M., Iwabe, N., Miyata, T., Hosoya, T., Masai, I., and Hotta, Y. 1994. Isolation and characterization of a gene for a ryanodine receptor/calcium release channel in Drosophila melanogaster. FEBS Lett. 337: 81-87.
32. Taylor, D.A., Sack, J.S., Maune, J.F., Beckingham, K., and Quiocho, F.A. 1991, Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-Å resolution. J. Biol. Chem. 266: 21375-21380.
33. Tohtong, R., Yamashita, H., Graham, M., Haeberle, J., Simcox, A., and Maughan, D, 1995. Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain. Nature 374: 650-653.
34. 2+ release channel (ryanodine receptor). Biophys. J. 69: 106-119.
35. Van Eldik, L. and Watterson, D.M. 1998. Calmodulin and signal transduction. Academic Press, San Diego, CA.
36. VanScyoc, W.S. and Shea, M.A. 2001. Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder. Protein Sci. 10: 1758-1768.
37. VanScyoc, W.S., Sorensen, B.R., Rusinova, E., Laws, W.R., Ross, J.B., and Shea, M.A. 2002. Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence. Biophys. J. 83: 2767-2780.
38. Wang, B., Sullivan, K.M.C., and Beckingham, K. 2003. Drosophila calmodulin mutants with specific defects in the musculature or in the nervous system. Genetics 165: 1255-1268.
39. Xiong, L.W., Newman, R.A., Rodney, G.G., Thomas, O., Zhang, J.Z., Persechini, A., Shea, M.A., and Hamilton, S.L. 2002. Lobe-dependent regulation of ryanodine receptor type 1 by calmodulin. J. Biol. Chem. 277: 40862-40870.
40. 2+-pumping in native cardiac sarcoplasmic reticulum. Biochem. Biophys. Res. Commun. 258: 66-72.
41. 2+/ calmodulin-dependent protein kinase. J. Biol. Chem. 268: 8394-8397.
42. Zdarek, J. and Fraenkel, G. 1972. The mechanism of puparium formation in flies. J. Exp. Zool. 179: 315-323.
43. Zhang, M., Tanaka, T., and Ikura, M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2: 758-767.
44. 2+ binding sites of calmodulin are critical for the regulation of myosin 1 β motor function. J. Biol. Chem. 273: 20481-20486.
45. Zuhlke, R.D., Pitt, G.S., Deisseroth, K., Tsien, R.W., and Reuter, H. 1999. Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature 399: 159-162.