Skip to main content
SpringerLink
Log in

A strange calmodulin of yeast

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Calmodulin of Saccharomyces cerevisiae has different Ca2+ binding properties from other calmodulins. We previously reported that the maximum number of Ca2+ binding was 3 mol/mol and the fourth binding site was defective, which was different from 4 mol/mol for others. Their macroscopic dissociation constants suggested the cooperative three Ca2+ bindings rather than a pair of cooperative two Ca2+ bindings of ordinary calmodulin. Here we present evidence for yeast calmodulin showing the intramolecular close interaction between the N-terminal half domain and the C-terminal half domain, while the two domains of ordinary calmodulin are independent of each other. We will discuss the relationship of the shape and the shape change caused by the Ca2+ binding to the enzyme activation in yeast. The functional feature of calmodulin in yeast will also be considered, which might be different from the one of vertebrate calmodulin.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Kakiuchi S, Yamazaki R, Nakajima H: Properties of a heat-stable phosphodiesterase activating factor isolated from brain extract. Proc Japan Acad 46: 587–592, 1970

    Google Scholar 

  2. Cheung WY: Cyclic 3′,5′-nucleotide phosphodiesterase. Demonstration of an activator. Biochem Biophys Res Commun 38: 533–538, 1970

    Google Scholar 

  3. Teo TS, Wang JH: Mechanism of activation of a cyclic adenosine 3′,5′-monophosphate phosphodiesterase from bovine heart by calcium ions. Identification of the protein activator as a Ca2+ binding protein. J Biol Chem 248: 5950–5955, 1973

    Google Scholar 

  4. Ebashi S, Kodama A: A new protein factor promoting aggregation of tropomyosin. J Biochem 58: 107–108, 1965

    Google Scholar 

  5. Ebashi S: Calcium binding and relaxation in the actomyosin system. J Biochem 48: 150–151, 1960

    Google Scholar 

  6. Yazawa M, Yagi K: A calcium-binding subunit of myosin light chain kinase. J Biochem 82: 287–289, 1977

    Google Scholar 

  7. Yagi K, Yazawa M, Kakiuchi S, Ohshima M, Uenishi K: Identification of an activator protein for myosin light chain kinase as the Ca2+-dependent modulator protein. J Biol Chem 253: 1338–1340, 1978

    Google Scholar 

  8. Ebashi S, Endo M: Calcium ion and muscle contraction. Prog Biophys Mol Biol 18: 123–183, 1968

    Google Scholar 

  9. Ozawa E: Activation of muscular phosphorylase b kinase by a minute amount of Ca ion. J Biochem 71: 321–331, 1972

    Google Scholar 

  10. Brostrom CO, Hunkeler FL, Krebs EG: The regulation of skeletal muscle phosphorylase kinase by Ca2+. J Biol Chem 246: 1961–1967, 1971

    Google Scholar 

  11. Cohen P, Burchell A, Foulkes JG, Cohen PTW, Vanaman TC, Nairn AC: Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett 92: 287–293, 1978

    Google Scholar 

  12. Stewart AA, Ingebritsen TS, Manalan A, Klee CB, Cohen P: Discovery of a Ca2+-and calmodulin-dependent protein phosphatase. FEBS Lett 137: 80–84, 1982

    Google Scholar 

  13. Klee CB, Vanaman TC: Calmodulin. Adv Protein Chem 35: 213–321, 1982

    Google Scholar 

  14. Kretsinger RH, Nockolds CE: Carp muscle calcium-binding protein. II. Structure determination and general description. J Biol Chem 248: 3313–3326, 1973

    Google Scholar 

  15. Toda H, Yazawa M, Sakiyama F, Yagi K: Amino acid sequence of calmodulin from wheat germ. J Biochem 98: 833–842, 1985

    Google Scholar 

  16. Babu YS, Bugg CE, Cook WJ: Structure of calmodulin refined at 2.2 Å resolution. J Mol Biol 204: 191–204, 1988

    Google Scholar 

  17. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A: Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256: 632–638, 1992

    Google Scholar 

  18. Meador WE, Means AR, Quiocho FA: Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257: 1251–1255, 1992

    Google Scholar 

  19. Barbato G, Ikura M, Kay LE, Pastor RW, Bax A: Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31: 5269–5278, 1992

    Google Scholar 

  20. Tjandra N, Kuboniwa H, Ren H, Bax A: Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements. Eur J Biochem 230: 1014–1024, 1995

    Google Scholar 

  21. Zhang M, Tanaka T, Ikura M: Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct Biol 2: 758–767, 1995

    Google Scholar 

  22. Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Mee CB, Bax A: Solution structure of calcium-free calmodulin. Nature Struct Biol 2: 768–776, 1995

    Google Scholar 

  23. Ikura M: Calcium binding and conformational response in EF-hand proteins. Trends Biochem Sci 21: 14–17, 1996

    Google Scholar 

  24. Walsh M, Stevens FC, Kuznicki J, Drabikowski W: Characterization of tryptic fragments obtained from bovine brain protein modulator of cyclic nucleotide phosphodiesterase. J Biol Chem 252: 7440–7443, 1977

    Google Scholar 

  25. Drabikowski W, Brzeska H, Venyaminov SY: Tryptic fragments of calmodulin. Ca2+-and Mg2+-induced conformational changes. J Biol Chem 257: 11584–11590, 1982

    Google Scholar 

  26. Minowa O, Yagi K: Calcium binding to tryptic fragments of calmodulin. J Biochem 96: 1175–1182, 1984

    Google Scholar 

  27. Vogel HJ, Lindahl L, Thulin E: Calcium-dependent hydrophobic interaction chromatography of calmodulin, troponin C and their proteolytic fragments. FEBS Lett 157: 241–246, 1983

    Google Scholar 

  28. Brzeska H, Szynkiewicz J, Drabikowski W: Localization of hydrophobic sites in calmodulin and skeletal muscle troponin C studied using tryptic fragments. A simple method of their preparation. Biochem Biophys Res Commun 115: 87–93, 1983

    Google Scholar 

  29. Nakamura T, Fujita K, Eguchi Y, Yazawa M: Properties of calciumdependent regulatory proteins from fungi and yeast. J Biochem 95: 1551–1557, 1984

    Google Scholar 

  30. Luan Y, Matsuura I, Yazawa M, Nakamura T, Yagi K: Yeast calmodulin: Structural and functional differences compared with vertebrate calmodulin. J Biochem 102: 1531–1537, 1987

    Google Scholar 

  31. Matsuura I, Ishihara K, Nakai Y, Yazawa M, Toda H, Yagi K: A site-directed mutagenesis study of yeast calmodulin. J Biochem 109: 190–197, 1991

    Google Scholar 

  32. Matsuura I, Kimura E, Tai K, Yazawa M: Mutagenesis of the fourth calcium binding domain of yeast calmodulin. J Biol Chem 268: 13267–13273, 1993

    Google Scholar 

  33. Ohya Y, Uno I, Ishikawa T, Anraku Y: Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae. Eur J Biochem 168: 13–19, 1987

    Google Scholar 

  34. Yoshino H, Izumi Y, Sakai K, Takezawa H, Matsuura I, Maekawa H, Yazawa M: Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: Implications for structure/function. Biochemistry 35: 2388–2393, 1996

    Google Scholar 

  35. Starovasnik MA, Davis TN, Klevit RE: 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 32: 3261–3270, 1993

    Google Scholar 

  36. Nakashima K, Maekawa H, Yazawa M: Chimeras of yeast and chicken calmodulin demonstrate differences in activation mechanisms of target enzymes. Biochemistry 35: 5602–5610, 1996

    Google Scholar 

  37. Davis TN, Urdea MS, Masiarz FR, Thorner J: Isolation of the yeast calmodulin gene: Calmodulin is an essential protein. Cell 47: 423–431, 1986

    Google Scholar 

  38. Sun GH, Ohya Y, Anraku Y: Half-calmodulin is sufficient for cell proliferation. Expression of N-and C-terminal halves of calmodulin in the yeast Saccharomyces cerevisiae. J Biol Chem 266: 7008–7015, 1991

    Google Scholar 

  39. Flaherty KM, Zozulya S, Stryer L, McKay DB: Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75: 709–716, 1993

    Google Scholar 

  40. Griffith JP, Kim JL, Kim EE, Sintchak MD, Thomson JA, Fitzgibbon MJ, Fleming MA, Caron PR, Hsiao K, Navia MA: X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell 82: 507–522, 1995

    Google Scholar 

  41. Ohya Y, Anraku Y: Functional expression of chicken calmodulin in yeast. Biochem Biophys Res Commun 158: 541–547, 1989

    Google Scholar 

  42. Yazawa M, Ikura M, Hikichi K, Luan Y, Yagi K: Communication between two globular domains of calmodulin in the presence of mastoparan or caldesmon fragment. J Biol Chem 262: 10951–10954, 1987

    Google Scholar 

  43. Strynadka NW, James MNG: Crystal structures of the helix-loop-helix calcium-binding proteins. Annu Rev Biochem 58: 951–998, 1989

    Google Scholar 

  44. Rayment I, Rypniewski WR, Schmidt-Bäse K, Smith R, Tomchick DR, Benning MM, Winkelmann DA, Wesenberg G, Holden HM: Three-dimensional structure of myosin subfragment-l: A molecular motor. Science 261: 50–58, 1993

    Google Scholar 

  45. Houdusse A, Cohen C: Target sequence recognition by the calmodulin superfamily: Implications from light chain binding to the regulatory domain of scallop myosin. Proc Natl Acad Sci USA 92: 10644–10647, 1995

    Google Scholar 

  46. Cook WJ, Jeffrey LC, Cox JA, Vijay-Kumar S: Structure of sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J Mol Biol 229: 461–471, 1993

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo, Japan

    Michio Yazawa & Ken-ichi Nakashima

  2. Agroscience Research Laboratory, Hokkai Sankyo Co. Ltd., Kitahiroshima, Japan

    Koichi Yagi

Authors
  1. Michio Yazawa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ken-ichi Nakashima
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Koichi Yagi
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yazawa, M., Nakashima, Ki. & Yagi, K. A strange calmodulin of yeast. Mol Cell Biochem 190, 47–54 (1999). https://doi.org/10.1023/A:1006951710440

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1006951710440

Search

Navigation