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Volumn 317, Issue 2, 2004, Pages 428-436

Calmodulin-binding proteins in bryophytes: Identification of abscisic acid-, cold-, and osmotic stress-induced genes encoding novel membrane-bound transporter-like proteins

Author keywords

Abscisic acid; Bryophytes; Ca2+; Calmodulin; Freezing tolerance; Ion transporter; Low temperature; Osmotic stress; Physcomitrella patens

Indexed keywords

ABSCISIC ACID; AMPHOPHILE; CALCIUM ACTIVATED POTASSIUM CHANNEL; CALMODULIN; CARRIER PROTEIN; HORMONE; MEMBRANE TRANSPORTING PROTEIN MCAMB 1; MEMBRANE TRANSPORTING PROTEIN MCAMB 2; UNCLASSIFIED DRUG;

EID: 1842426646     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.03.052     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D., Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 10:2000;322-328.
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 3
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • Saimi Y., Kung C. Calmodulin as an ion channel subunit. Ann. Rev. Physiol. 64:2002;289-311.
    • (2002) Ann. Rev. Physiol. , vol.64 , pp. 289-311
    • Saimi, Y.1    Kung, C.2
  • 4
    • 0030218118 scopus 로고    scopus 로고
    • Calmodulin regulation of cyclic nucleotide-gated channels
    • Molday R.S. Calmodulin regulation of cyclic nucleotide-gated channels. Curr. Opin. Neurobiol. 8:1996;445-452.
    • (1996) Curr. Opin. Neurobiol. , vol.8 , pp. 445-452
    • Molday, R.S.1
  • 5
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with NR1 subunit
    • Ehlers M.D., Zhang S., Bernhardt J.P., Huganir R.L. Inactivation of NMDA receptors by direct interaction of calmodulin with NR1 subunit. Cell. 84:1996;745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhardt, J.P.3    Huganir, R.L.4
  • 12
    • 0025016198 scopus 로고
    • Calmodulin activation of calcium-dependent sodium channels in excised membrane patches of Paramecium
    • Saimi Y., Ling K.Y. Calmodulin activation of calcium-dependent sodium channels in excised membrane patches of Paramecium. Science. 249:1990;1441-1444.
    • (1990) Science , vol.249 , pp. 1441-1444
    • Saimi, Y.1    Ling, K.Y.2
  • 14
    • 0035877761 scopus 로고    scopus 로고
    • Identification of common binding sites for calmodulin and inositol 1,4,5-triphosphate receptors on the carboxyl termini of Trp channels
    • Tang J., Lin Y., Zhang Z., Tikunova S., Birnbaumer L., Zhu M.X. Identification of common binding sites for calmodulin and inositol 1,4,5-triphosphate receptors on the carboxyl termini of Trp channels. J. Biol. Chem. 276:2001;21303-21310.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21303-21310
    • Tang, J.1    Lin, Y.2    Zhang, Z.3    Tikunova, S.4    Birnbaumer, L.5    Zhu, M.X.6
  • 15
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich K.P., Ikura M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell. 108:2002;739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 16
    • 0026419945 scopus 로고
    • Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium
    • Knight M.R., Campbell A.K., Smith S.M., Trewavas A.J. Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium. Nature. 352:1991;524-526.
    • (1991) Nature , vol.352 , pp. 524-526
    • Knight, M.R.1    Campbell, A.K.2    Smith, S.M.3    Trewavas, A.J.4
  • 17
    • 0031279985 scopus 로고    scopus 로고
    • Calcium signaling in Arabidopsis thaliana responding to drought and salinity
    • Knight H., Trewavas A.J., Knight M.R. Calcium signaling in Arabidopsis thaliana responding to drought and salinity. Plant J. 12:1997;1067-1078.
    • (1997) Plant J. , vol.12 , pp. 1067-1078
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 18
    • 0033152627 scopus 로고    scopus 로고
    • Temperature sensing by plants: The primary characteristics of signal perception and calcium response
    • Plieth C., Hansen U.P., Knight H., Knight M.R. Temperature sensing by plants: the primary characteristics of signal perception and calcium response. Plant J. 18:1999;491-497.
    • (1999) Plant J. , vol.18 , pp. 491-497
    • Plieth, C.1    Hansen, U.P.2    Knight, H.3    Knight, M.R.4
  • 20
    • 0039795372 scopus 로고
    • Cytosolic calcium regulates ion channels in the plasma membrane of Vicia faba guard cells
    • Schroeder J.I., Hagiwara S. Cytosolic calcium regulates ion channels in the plasma membrane of Vicia faba guard cells. Nature. 338:1989;427-430.
    • (1989) Nature , vol.338 , pp. 427-430
    • Schroeder, J.I.1    Hagiwara, S.2
  • 21
    • 0027977519 scopus 로고
    • + channels and calcium-induced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure
    • + channels and calcium-induced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure. Plant Cell. 6:1994;669-683.
    • (1994) Plant Cell , vol.6 , pp. 669-683
    • Ward, J.M.1    Schroeder, J.I.2
  • 22
    • 0028139683 scopus 로고
    • 2+-calmodulin modulates ion channel activity in storage protein vacuoles of barley aleurone cells
    • 2+-calmodulin modulates ion channel activity in storage protein vacuoles of barley aleurone cells. Plant Cell. 6:1994;277-285.
    • (1994) Plant Cell , vol.6 , pp. 277-285
    • Bethke, P.C.1    Jones, R.L.2
  • 23
    • 0032539554 scopus 로고    scopus 로고
    • Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone
    • Schuurink R.C., Shartzer S.F., Fath A., Jones R.L. Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone. Proc. Natl. Acad. Sci. USA. 95:1998;1044-1949.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1044-1949
    • Schuurink, R.C.1    Shartzer, S.F.2    Fath, A.3    Jones, R.L.4
  • 24
    • 0343358891 scopus 로고    scopus 로고
    • Characterization of a novel gene family of putative cyclic nucleotide- and calmodulin-regulated ion channels in Arabidopsis thaliana
    • Köhler C., Merkle T., Neuhaus G. Characterization of a novel gene family of putative cyclic nucleotide- and calmodulin-regulated ion channels in Arabidopsis thaliana. Plant J. 18:1999;97-104.
    • (1999) Plant J. , vol.18 , pp. 97-104
    • Köhler, C.1    Merkle, T.2    Neuhaus, G.3
  • 25
    • 0038715131 scopus 로고    scopus 로고
    • Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel
    • Hua B.G., Mercier R.W., Leng Q., Berkowitz G.A. Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel. Plant Physiol. 132:2003;1353-1362.
    • (2003) Plant Physiol. , vol.132 , pp. 1353-1362
    • Hua, B.G.1    Mercier, R.W.2    Leng, Q.3    Berkowitz, G.A.4
  • 26
    • 0001383199 scopus 로고
    • Analysis of gametophytic development in the moss Physcomitrella patens, using auxin and cytokinin resistant mutants
    • Ashton N.W., Grimsely N.H., Cove D.J. Analysis of gametophytic development in the moss Physcomitrella patens, using auxin and cytokinin resistant mutants. Planta. 144:1979;427-435.
    • (1979) Planta , vol.144 , pp. 427-435
    • Ashton, N.W.1    Grimsely, N.H.2    Cove, D.J.3
  • 27
    • 0038244053 scopus 로고    scopus 로고
    • Abscisic acid-induced freezing tolerance in the moss Physcomitrella patens is accompanied by increased expression of stress-related genes
    • Minami A., Nagao M., Arakawa K., Fujikawa S., Takezawa D. Abscisic acid-induced freezing tolerance in the moss Physcomitrella patens is accompanied by increased expression of stress-related genes. J. Plant Physiol. 160:2003;475-483.
    • (2003) J. Plant Physiol. , vol.160 , pp. 475-483
    • Minami, A.1    Nagao, M.2    Arakawa, K.3    Fujikawa, S.4    Takezawa, D.5
  • 28
    • 51249167396 scopus 로고
    • 35S-labeled recombinant calmodulin as a probe
    • 35S-labeled recombinant calmodulin as a probe. Plant Mol. Biol. Rep. 10:1993;199-206.
    • (1993) Plant Mol. Biol. Rep. , vol.10 , pp. 199-206
    • Fromm, H.1    Chua, N.H.2
  • 29
    • 0141620376 scopus 로고    scopus 로고
    • Characterization of a novel plant PP2C-like protein Ser/Thr phosphatase as a calmodulin-binding protein
    • Takezawa D. Characterization of a novel plant PP2C-like protein Ser/Thr phosphatase as a calmodulin-binding protein. J. Biol. Chem. 278:2003;38076- 38083.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38076-38083
    • Takezawa, D.1
  • 30
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 31
    • 0027145921 scopus 로고
    • Isolation and characterization of two cDNAs that encode for calmodulin-binding proteins from corn root tips
    • Reddy A.S.N., Takezawa D., Fromm H., Poovaiah B.W. Isolation and characterization of two cDNAs that encode for calmodulin-binding proteins from corn root tips. Plant Sci. 94:1993;109-117.
    • (1993) Plant Sci. , vol.94 , pp. 109-117
    • Reddy, A.S.N.1    Takezawa, D.2    Fromm, H.3    Poovaiah, B.W.4
  • 32
    • 0031058901 scopus 로고    scopus 로고
    • Characterization of the basic amphiphilic-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein
    • Dash S., Niemaczura W., Harrington H.M. Characterization of the basic amphiphilic-helix calmodulin-binding domain of a 61.5. kDa tobacco calmodulin-binding protein Biochemistry. 36:1997;2025-2029.
    • (1997) Biochemistry , vol.36 , pp. 2025-2029
    • Dash, S.1    Niemaczura, W.2    Harrington, H.M.3
  • 33
    • 0027278759 scopus 로고
    • A myosin-like protein from a higher plant
    • Knight A.E., Kendrick-Jones J. A myosin-like protein from a higher plant. J. Mol. Biol. 231:1993;148-154.
    • (1993) J. Mol. Biol. , vol.231 , pp. 148-154
    • Knight, A.E.1    Kendrick-Jones, J.2
  • 34
    • 0026712329 scopus 로고
    • A region of antisense RNA from human p120 cDNA with high homology to mouse p120 cDNA inhibits NIH 3T3 proliferation
    • Valdez B.C., Perlaky L., Saijo Y., Henning D., Zhu C., Busch R.K., Zhang W.W., Busch H. A region of antisense RNA from human p120 cDNA with high homology to mouse p120 cDNA inhibits NIH 3T3 proliferation. Cancer Res. 52:1992;5681-5686.
    • (1992) Cancer Res. , vol.52 , pp. 5681-5686
    • Valdez, B.C.1    Perlaky, L.2    Saijo, Y.3    Henning, D.4    Zhu, C.5    Busch, R.K.6    Zhang, W.W.7    Busch, H.8
  • 36
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 38
    • 0028895950 scopus 로고
    • Cation selectivity in ion channels
    • Kerr I.D., Sansom M.S. Cation selectivity in ion channels. Nature. 373:1995;112.
    • (1995) Nature , vol.373 , pp. 112
    • Kerr, I.D.1    Sansom, M.S.2
  • 40
    • 12044259918 scopus 로고
    • Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression: Evidence for a role of calcium
    • Monroy A.F., Sarhan F., Dhindsa R.S. Cold-induced changes in freezing tolerance, protein phosphorylation, and gene expression: evidence for a role of calcium. Plant Physiol. 102:1993;1227-1235.
    • (1993) Plant Physiol. , vol.102 , pp. 1227-1235
    • Monroy, A.F.1    Sarhan, F.2    Dhindsa, R.S.3
  • 41
    • 0033230738 scopus 로고    scopus 로고
    • Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco
    • van Der Luit A.H., Olivari C., Haley A., Knight M.R., Trewavas A.J. Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco. Plant Physiol. 121:1999;705-714.
    • (1999) Plant Physiol. , vol.121 , pp. 705-714
    • Van Der Luit, A.H.1    Olivari, C.2    Haley, A.3    Knight, M.R.4    Trewavas, A.J.5
  • 42
    • 0030139945 scopus 로고    scopus 로고
    • The moss, Physcomitrella patens, transformed with apoaequorin cDNA responds to cold shock, mechanical perturbation and pH with transient increases in cytoplasmic calcium
    • Russell A.J., Knight M.R., Cove D.J., Knight C.D., Trewavas A.J., Wang T.L. The moss, Physcomitrella patens, transformed with apoaequorin cDNA responds to cold shock, mechanical perturbation and pH with transient increases in cytoplasmic calcium. Transgenic Res. 5:1996;167-170.
    • (1996) Transgenic Res. , vol.5 , pp. 167-170
    • Russell, A.J.1    Knight, M.R.2    Cove, D.J.3    Knight, C.D.4    Trewavas, A.J.5    Wang, T.L.6


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