메뉴 건너뛰기




Volumn 57, Issue 15, 2006, Pages 4245-4255

Structural and functional diversity within the cystatin gene family of Hordeum vulgare

Author keywords

Antifungal activity; Barley cystatin genes; Cysteine proteinase inhibitor; Intron exon structure; Three dimensional structure prediction

Indexed keywords

CRYSTAL STRUCTURE; DNA; ENZYME KINETICS; GENES; HORMONES; PROTEINS;

EID: 33845605556     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/erl200     Document Type: Article
Times cited : (43)

References (48)
  • 1
    • 0028093536 scopus 로고
    • Corn cystatin I expressed in Escherichia coli: Investigation of its inhibitory profile and occurrence in corn kernels
    • Abe M, Abe K, Iwabuchi K, Domoto C, Arai S. 1994. Corn cystatin I expressed in Escherichia coli: investigation of its inhibitory profile and occurrence in corn kernels. Journal of Biochemistry 116, 488-492.
    • (1994) Journal of Biochemistry , vol.116 , pp. 488-492
    • Abe, M.1    Abe, K.2    Iwabuchi, K.3    Domoto, C.4    Arai, S.5
  • 2
    • 33845654047 scopus 로고    scopus 로고
    • Effects of potato plants expressing a barley cystatin on the predatory bug Podisus maculiventris via herbivorous prey feeding on the plant
    • (in press)
    • Alvarez-Alfageme F, Martinez M, Pascual-Ruiz S, Castañera P, Diaz I, Ortego F. 2006. Effects of potato plants expressing a barley cystatin on the predatory bug Podisus maculiventris via herbivorous prey feeding on the plant. Transgenic Research (in press).
    • (2006) Transgenic Research
    • Alvarez-Alfageme, F.1    Martinez, M.2    Pascual-Ruiz, S.3    Castañera, P.4    Diaz, I.5    Ortego, F.6
  • 3
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin): Homology with animal cystatins and transient expression in the ripening process of rice seeds
    • Abe K, Emori Y, Kondo H, Suzuki K, Arai S. 1987a. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin): homology with animal cystatins and transient expression in the ripening process of rice seeds. Journal of Biological Chemistry 262, 16793-16797.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 4
    • 85004645817 scopus 로고
    • Purification and characterization of a rice cysteine proteinase inhibitor
    • Abe K, Kondo H, Arai S. 1987b. Purification and characterization of a rice cysteine proteinase inhibitor. Agricultural and Biological Chemistry 51, 2763-2768.
    • (1987) Agricultural and Biological Chemistry , vol.51 , pp. 2763-2768
    • Abe, K.1    Kondo, H.2    Arai, S.3
  • 6
    • 3242885247 scopus 로고    scopus 로고
    • Prototype demonstration of transgenic resistance to the nematode Radopholus similes conferred on banana by a cystatin
    • Atkinson HJ, Grimwood S, Johnston K, Green J. 2004. Prototype demonstration of transgenic resistance to the nematode Radopholus similes conferred on banana by a cystatin. Transgenic Research 13, 135-142.
    • (2004) Transgenic Research , vol.13 , pp. 135-142
    • Atkinson, H.J.1    Grimwood, S.2    Johnston, K.3    Green, J.4
  • 9
    • 33646429223 scopus 로고    scopus 로고
    • A cold inducible multidomain cystatin from winter wheat inhibits growth of the mold fungus, Microdochium nivale
    • Christova PK, Christov NK, Imai R. 2006. A cold inducible multidomain cystatin from winter wheat inhibits growth of the mold fungus, Microdochium nivale. Planta 223, 1207-1218.
    • (2006) Planta , vol.223 , pp. 1207-1218
    • Christova, P.K.1    Christov, N.K.2    Imai, R.3
  • 13
    • 0032787406 scopus 로고    scopus 로고
    • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants
    • Gutierrez-Campos R, Torres-Acosta J, Saucedo-Arias LJ, Gomez-Lim MA. 1999. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nature Biotechnology 17, 1223-1226.
    • (1999) Nature Biotechnology , vol.17 , pp. 1223-1226
    • Gutierrez-Campos, R.1    Torres-Acosta, J.2    Saucedo-Arias, L.J.3    Gomez-Lim, M.A.4
  • 14
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: Natural and engineered phytoprotection
    • Haq SK, Atif SM, Khan RH. 2004. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Archives of Biochemistry and Biophysics 431, 145-159.
    • (2004) Archives of Biochemistry and Biophysics , vol.431 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 15
    • 0041402695 scopus 로고    scopus 로고
    • Functional comparison of homologous members of three groups of Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.)
    • Heibges A, Salamini F, Gebhardt C. 2003. Functional comparison of homologous members of three groups of Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.). Molecular Genetics and Genomics 269, 535-541.
    • (2003) Molecular Genetics and Genomics , vol.269 , pp. 535-541
    • Heibges, A.1    Salamini, F.2    Gebhardt, C.3
  • 16
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22, 4673-4680.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 18
    • 0034616079 scopus 로고    scopus 로고
    • A plant defensive cystatin (soyacystatin) targets cathepsin L-like digestive cysteine proteinases (DvCALs) in the larval midgut of western corn rootworm (Diabrotica virgifera virgifera)
    • Koiwa H, Shade RE, Zhu-Salzman K, D'Urzo MP, Murdock LL, Bressan RA, Hasegawa PM. 2000. A plant defensive cystatin (soyacystatin) targets cathepsin L-like digestive cysteine proteinases (DvCALs) in the larval midgut of western corn rootworm (Diabrotica virgifera virgifera). FEBS Letters 471, 67-70.
    • (2000) FEBS Letters , vol.471 , pp. 67-70
    • Koiwa, H.1    Shade, R.E.2    Zhu-Salzman, K.3    D'Urzo, M.P.4    Murdock, L.L.5    Bressan, R.A.6    Hasegawa, P.M.7
  • 19
    • 0025160575 scopus 로고
    • Two distinct cystatin species in rice seeds with different specificities against cysteine poteinases
    • Kondo H, Abe K, Nishimura I, Watanabe H, Emori Y, Arai S. 1990. Two distinct cystatin species in rice seeds with different specificities against cysteine poteinases. Journal of Biological Chemistry 265, 5832-5837.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 5832-5837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 20
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. 2004. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinformatics 5, 150-163.
    • (2004) Brief Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 22
    • 0000155139 scopus 로고
    • Molecular cloning of complementary DNA encoding the lignin forming peroxidase from tobacco: Molecular analysis and tissue-specific expression
    • Lagrimini LM, Burkhart W, Moyer M, Rosthein S. 1987. Molecular cloning of complementary DNA encoding the lignin forming peroxidase from tobacco: molecular analysis and tissue-specific expression. Proceedings of the National Academy of Sciences, USA 84, 7542-7546.
    • (1987) Proceedings of the National Academy of Sciences, USA , vol.84 , pp. 7542-7546
    • Lagrimini, L.M.1    Burkhart, W.2    Moyer, M.3    Rosthein, S.4
  • 24
    • 21544454156 scopus 로고    scopus 로고
    • Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley
    • Martinez M, Abraham Z, Carbonero P, Diaz I. 2005a. Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley. Molecular Genetics and Genomics 273, 423-432.
    • (2005) Molecular Genetics and Genomics , vol.273 , pp. 423-432
    • Martinez, M.1    Abraham, Z.2    Carbonero, P.3    Diaz, I.4
  • 26
    • 17344392459 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic fungi by the barley cystatin HvCPI (gene Icy) is not associated with its cysteine proteinase inhibitory properties
    • Martinez M, Lopez-Solanilla E, Rodriguez-Palenzuela P, Carbonero P, Diaz I. 2003a. Inhibition of plant-pathogenic fungi by the barley cystatin HvCPI (gene Icy) is not associated with its cysteine proteinase inhibitory properties. Molecular Plant-Microbe Interactions 16, 876-883.
    • (2003) Molecular Plant-Microbe Interactions , vol.16 , pp. 876-883
    • Martinez, M.1    Lopez-Solanilla, E.2    Rodriguez-Palenzuela, P.3    Carbonero, P.4    Diaz, I.5
  • 27
    • 0037338198 scopus 로고    scopus 로고
    • A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves
    • Martinez M, Rubio-Somoza I, Carbonero P, Diaz I. 2003b. A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves. Journal of Experimental Botany 54, 951-959.
    • (2003) Journal of Experimental Botany , vol.54 , pp. 951-959
    • Martinez, M.1    Rubio-Somoza, I.2    Carbonero, P.3    Diaz, I.4
  • 31
    • 0029762217 scopus 로고    scopus 로고
    • Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin
    • Misaka T, Kuroda M, Abuchi K, Abe K, Arai S. 1996. Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin. European Journal of Biochemistry 240, 609-614.
    • (1996) European Journal of Biochemistry , vol.240 , pp. 609-614
    • Misaka, T.1    Kuroda, M.2    Abuchi, K.3    Abe, K.4    Arai, S.5
  • 32
    • 0034610303 scopus 로고    scopus 로고
    • Three-dimensional solution of oryzacystatin-I, a cysteine proteinase inhibitor of rice, Oryza sativa L. japonica
    • Nagata K, Kudo N, Abe K, Arai S, Tanokura M. 2000. Three-dimensional solution of oryzacystatin-I, a cysteine proteinase inhibitor of rice, Oryza sativa L. japonica. Biochemistry 39, 14753-14760.
    • (2000) Biochemistry , vol.39 , pp. 14753-14760
    • Nagata, K.1    Kudo, N.2    Abe, K.3    Arai, S.4    Tanokura, M.5
  • 34
    • 0029004590 scopus 로고
    • Protein modeling by e-mail
    • Peitsch M. 1995. Protein modeling by e-mail. Biotechnology 13, 658-660.
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.1
  • 35
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modeling
    • Peitsch M. 1996. ProMod and Swiss-Model: internet-based tools for automated comparative protein modeling. Biochemical Society Transactions 224, 274-279.
    • (1996) Biochemical Society Transactions , vol.224 , pp. 274-279
    • Peitsch, M.1
  • 37
    • 0032406093 scopus 로고    scopus 로고
    • A chestnut seed cystatin differentially effective against cysteine proteinases from closely related pests
    • Pernas M, Sanchez-Monge R, Gomez L, Salcedo G. 1998. A chestnut seed cystatin differentially effective against cysteine proteinases from closely related pests. Plant Molecular Biology 38, 1235-1242.
    • (1998) Plant Molecular Biology , vol.38 , pp. 1235-1242
    • Pernas, M.1    Sanchez-Monge, R.2    Gomez, L.3    Salcedo, G.4
  • 38
    • 0033947715 scopus 로고    scopus 로고
    • Der p1 and der f1, the highly related and major allergens from house mites, are differentially affected by a plant cystatin
    • Pernas M, Sanchez-Monge R, Lombardero M, Ateaga C, Castañera P, Salcedo G. 2000. Der p1 and Der f1, the highly related and major allergens from house mites, are differentially affected by a plant cystatin. Clinical Experimental Allergy 30, 972-978.
    • (2000) Clinical Experimental Allergy , vol.30 , pp. 972-978
    • Pernas, M.1    Sanchez-Monge, R.2    Lombardero, M.3    Ateaga, C.4    Castañera, P.5    Salcedo, G.6
  • 39
    • 10744227034 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a novel type of Bowman-Birk inhibitor gene family in rice
    • Qu L-J, Chen J, Liu M, et al. 2003. Molecular cloning and functional analysis of a novel type of Bowman-Birk inhibitor gene family in rice. Plant Physiology 133, 560-570.
    • (2003) Plant Physiology , vol.133 , pp. 560-570
    • Qu, L.-J.1    Chen, J.2    Liu, M.3
  • 45
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants
    • Solomon M, Belenghi B, Delledonne M, Levine A. 1999. The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants. The Plant Cell 11, 431-444.
    • (1999) The Plant Cell , vol.11 , pp. 431-444
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Levine, A.4
  • 46
    • 0002121649 scopus 로고
    • Isolation of plant DNA and RNA
    • Taylor B, Powell A. 1982. Isolation of plant DNA and RNA. Focus 4, 4-6.
    • (1982) Focus , vol.4 , pp. 4-6
    • Taylor, B.1    Powell, A.2
  • 47
    • 0033117381 scopus 로고    scopus 로고
    • Transgenic Arabidopsis leaf tissue expressing a modified oryzacystatin shows resistance to the field slug Deroceras reticulatum (Muller)
    • Walker AJ, Urwin PE, Atkinson HJ, Brain P, Glen DM, Shewry PR. 1999. Transgenic Arabidopsis leaf tissue expressing a modified oryzacystatin shows resistance to the field slug Deroceras reticulatum (Muller). Transgenic Research 8, 95-103.
    • (1999) Transgenic Research , vol.8 , pp. 95-103
    • Walker, A.J.1    Urwin, P.E.2    Atkinson, H.J.3    Brain, P.4    Glen, D.M.5    Shewry, P.R.6
  • 48
    • 21344450737 scopus 로고    scopus 로고
    • Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)
    • Yang AH, Yeh KW. 2005. Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1). Planta 221, 493-501.
    • (2005) Planta , vol.221 , pp. 493-501
    • Yang, A.H.1    Yeh, K.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.