메뉴 건너뛰기




Volumn 89, Issue 5, 2007, Pages 605-612

Seed defensins from T. kiharae and related species: Genome localization of defensin-encoding genes

Author keywords

Amino acid sequence; Antimicrobial peptides; Defensins; Triticum kiharae Dorof. et Migusch.; Wheat phylogeny

Indexed keywords

DEFENSIN;

EID: 34247632083     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.09.009     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 0029347190 scopus 로고
    • Plant defensins: novel antimicrobial peptides as components of the host defense system
    • Broekaert W.F., Terras F.R.G., Cammue B.P.A., and Osborn R.W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 108 (1995) 1353-1358
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 6
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobial polypeptides
    • Tossi A., and Sandri L. Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Design 8 (2002) 743-761
    • (2002) Curr. Pharm. Design , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 8
    • 23944488734 scopus 로고    scopus 로고
    • Plant γ-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins
    • Pelegrini P.B., and Franco O.L. Plant γ-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins. Int. J. Biochem. Cell Biol. 37 (2005) 2239-2253
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2239-2253
    • Pelegrini, P.B.1    Franco, O.L.2
  • 9
    • 13844322064 scopus 로고    scopus 로고
    • Defensins-components of the innate immune system in plants
    • Lay F.T., and Anderson M.A. Defensins-components of the innate immune system in plants. Curr. Protein Peptide Sci. 6 (2005) 85-101
    • (2005) Curr. Protein Peptide Sci. , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.A.2
  • 10
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-hordothionin, from barley endosperm
    • Mendez E., Moreno A., Colilla F.J., Pelaez F., Limas G.G., Mendez R., Soriano F., Salinas M., and de Haro C. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-hordothionin, from barley endosperm. J. Biochem 194 (1990) 533-539
    • (1990) J. Biochem , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.J.3    Pelaez, F.4    Limas, G.G.5    Mendez, R.6    Soriano, F.7    Salinas, M.8    de Haro, C.9
  • 11
    • 0025080513 scopus 로고
    • Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla F.J., Rocher A., and Mendez E. Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett. 270 (1990) 191-194
    • (1990) FEBS Lett. , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 12
    • 0027395308 scopus 로고
    • Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins
    • Bruix M., Jimenez M.A., Santoro J., Gonzalez C., Colilla F.J., Mendez E., and Rico M. Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry 32 (1993) 715-724
    • (1993) Biochemistry , vol.32 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3    Gonzalez, C.4    Colilla, F.J.5    Mendez, E.6    Rico, M.7
  • 16
    • 0346665520 scopus 로고    scopus 로고
    • Isolation and properties of floral defensins from ornamental tobacco and petunia
    • Lay F.T., Brugliera F., and Anderson M.A. Isolation and properties of floral defensins from ornamental tobacco and petunia. Plant Physiol 131 (2003) 1283-1293
    • (2003) Plant Physiol , vol.131 , pp. 1283-1293
    • Lay, F.T.1    Brugliera, F.2    Anderson, M.A.3
  • 18
    • 15644372264 scopus 로고    scopus 로고
    • Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity
    • De Samblanx G.W., Goderis I.J., Thevissen K., Raemaekers R., Fant F., Borremans F., et al. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. J. Biol. Chem. 272 (1997) 1171-1179
    • (1997) J. Biol. Chem. , vol.272 , pp. 1171-1179
    • De Samblanx, G.W.1    Goderis, I.J.2    Thevissen, K.3    Raemaekers, R.4    Fant, F.5    Borremans, F.6
  • 19
    • 0033668495 scopus 로고    scopus 로고
    • Fungal pathogen protection in potato by expression of a plant defensin peptide
    • Gao A.G., Hakimi S.M., Mittanck C.A., Wu Y., Woerner B.M., Stark D.M., et al. Fungal pathogen protection in potato by expression of a plant defensin peptide. Nat. Biotechnol 18 (2000) 1307-1310
    • (2000) Nat. Biotechnol , vol.18 , pp. 1307-1310
    • Gao, A.G.1    Hakimi, S.M.2    Mittanck, C.A.3    Wu, Y.4    Woerner, B.M.5    Stark, D.M.6
  • 20
    • 0028271965 scopus 로고
    • Pseudothionin-St1, a potato peptide active against potato pathogens
    • Moreno M., Segura A., and Garcia-Olmedo F. Pseudothionin-St1, a potato peptide active against potato pathogens. Eur. J. Biochem 223 (1994) 135-139
    • (1994) Eur. J. Biochem , vol.223 , pp. 135-139
    • Moreno, M.1    Segura, A.2    Garcia-Olmedo, F.3
  • 21
    • 0030935921 scopus 로고    scopus 로고
    • Fabatins: new antimicrobial plant peptides
    • Zhang Y., and Lewis K. Fabatins: new antimicrobial plant peptides. FEMS Microbiol. Lett. 149 (1997) 59-64
    • (1997) FEMS Microbiol. Lett. , vol.149 , pp. 59-64
    • Zhang, Y.1    Lewis, K.2
  • 22
    • 0029897150 scopus 로고    scopus 로고
    • Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems
    • Mendez E., Rocher A., Calero M., Girbes T., Citores L., and Soriano F. Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems. Eur. J. Biochem 239 (1996) 67-73
    • (1996) Eur. J. Biochem , vol.239 , pp. 67-73
    • Mendez, E.1    Rocher, A.2    Calero, M.3    Girbes, T.4    Citores, L.5    Soriano, F.6
  • 23
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat gamma-purothionins
    • Bloch C., and Richardson M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat gamma-purothionins. FEBS Lett. 279 (1991) 101-104
    • (1991) FEBS Lett. , vol.279 , pp. 101-104
    • Bloch, C.1    Richardson, M.2
  • 24
    • 0037260694 scopus 로고    scopus 로고
    • The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP
    • Lay F.T., Schirra H.J., Scanlon M.J., Anderson M.A., and Craig D.J. The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP. J. Mol. Biol. 325 (2003) 175-188
    • (2003) J. Mol. Biol. , vol.325 , pp. 175-188
    • Lay, F.T.1    Schirra, H.J.2    Scanlon, M.J.3    Anderson, M.A.4    Craig, D.J.5
  • 26
    • 0036681427 scopus 로고    scopus 로고
    • Inhibition of trypsin by cow-pea thionin: characterization, molecular modeling, and docking
    • Melo F.R., Ridgen D.J., Franco O.L., Mello L.V., Ary M.B., Grossi-de-Sa M.F., et al. Inhibition of trypsin by cow-pea thionin: characterization, molecular modeling, and docking. Proteins 48 (2002) 311-319
    • (2002) Proteins , vol.48 , pp. 311-319
    • Melo, F.R.1    Ridgen, D.J.2    Franco, O.L.3    Mello, L.V.4    Ary, M.B.5    Grossi-de-Sa, M.F.6
  • 27
    • 0034613541 scopus 로고    scopus 로고
    • Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin
    • Wijaya R., Neumann G.M., Condron R., Hughes A.B., and Polya G.M. Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci. 159 (2000) 243-255
    • (2000) Plant Sci. , vol.159 , pp. 243-255
    • Wijaya, R.1    Neumann, G.M.2    Condron, R.3    Hughes, A.B.4    Polya, G.M.5
  • 28
    • 4444295137 scopus 로고    scopus 로고
    • Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
    • Spelbrink R.G., Dilmac N., Allen A., Smith T.J., and Hockerman G.H. Differential antifungal and calcium channel-blocking activity among structurally related plant defensins. Plant Physiol 135 (2004) 2055-2067
    • (2004) Plant Physiol , vol.135 , pp. 2055-2067
    • Spelbrink, R.G.1    Dilmac, N.2    Allen, A.3    Smith, T.J.4    Hockerman, G.H.5
  • 29
    • 0032436013 scopus 로고    scopus 로고
    • Functional and structural features of gamma-zeathionins, a new class of sodium channel blockers
    • Kushmerick C., Castro M.D., Cruz J.S., Bloch C., and Beirao P.S.L. Functional and structural features of gamma-zeathionins, a new class of sodium channel blockers. FEBS Lett. 440 (1998) 302-306
    • (1998) FEBS Lett. , vol.440 , pp. 302-306
    • Kushmerick, C.1    Castro, M.D.2    Cruz, J.S.3    Bloch, C.4    Beirao, P.S.L.5
  • 32
    • 26944500600 scopus 로고    scopus 로고
    • Genome organization of more than 300 defensin-like genes in Arabidopsis
    • Silverstein K.A.T., Graham M.A., Paape T.D., and VandenBosch K.A. Genome organization of more than 300 defensin-like genes in Arabidopsis. Plant Physiol 138 (2005) 600-610
    • (2005) Plant Physiol , vol.138 , pp. 600-610
    • Silverstein, K.A.T.1    Graham, M.A.2    Paape, T.D.3    VandenBosch, K.A.4
  • 34
    • 0038663127 scopus 로고    scopus 로고
    • A novel family in Medicago truncatula consisting of more than 300 nodule-specific genes coding for small, secreted polypeptides with conserved cysteine motifs
    • Mergaert P., Nikovics K., Kelemen Z., Maunoury N., Vaubert D., Kondorosi A., and Kondorosi E. A novel family in Medicago truncatula consisting of more than 300 nodule-specific genes coding for small, secreted polypeptides with conserved cysteine motifs. Plant Physiol 132 (2003) 161-173
    • (2003) Plant Physiol , vol.132 , pp. 161-173
    • Mergaert, P.1    Nikovics, K.2    Kelemen, Z.3    Maunoury, N.4    Vaubert, D.5    Kondorosi, A.6    Kondorosi, E.7
  • 36
    • 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 J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , 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
  • 37
    • 0036399722 scopus 로고    scopus 로고
    • A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation
    • Koeke M., Okamoto T., Tsuda S., and Imai R. A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation. Biochem. Biophys. Res. Commun 298 (2002) 46-53
    • (2002) Biochem. Biophys. Res. Commun , vol.298 , pp. 46-53
    • Koeke, M.1    Okamoto, T.2    Tsuda, S.3    Imai, R.4
  • 38
    • 33646807759 scopus 로고    scopus 로고
    • Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids
    • Liu Y.-J., Cheng C.-S., Lai S.-M., Hsu M.-P., Chen C.-S., and Lyu P.-C. Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids. Proteins 63 (2006) 777-786
    • (2006) Proteins , vol.63 , pp. 777-786
    • Liu, Y.-J.1    Cheng, C.-S.2    Lai, S.-M.3    Hsu, M.-P.4    Chen, C.-S.5    Lyu, P.-C.6
  • 40
    • 0036301039 scopus 로고    scopus 로고
    • Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action
    • Almeida M.S., Cabral K.M.S., Kurtenbach E., Almeida F.C.L., and Valente A.P. Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. J. Mol. Biol. 315 (2002) 749-757
    • (2002) J. Mol. Biol. , vol.315 , pp. 749-757
    • Almeida, M.S.1    Cabral, K.M.S.2    Kurtenbach, E.3    Almeida, F.C.L.4    Valente, A.P.5
  • 41
    • 33746351784 scopus 로고    scopus 로고
    • Latarcins: Antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi(Zodariidae) exemplify biomolecular diversity
    • Kozlov S.A., Vassilevski A.A., Feofanov A.V., Surovoy A.Y., Karpunin D.V., and Grishin E.V. Latarcins: Antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi(Zodariidae) exemplify biomolecular diversity. J. Biol. Chem. 281 (2006) 20983-20992
    • (2006) J. Biol. Chem. , vol.281 , pp. 20983-20992
    • Kozlov, S.A.1    Vassilevski, A.A.2    Feofanov, A.V.3    Surovoy, A.Y.4    Karpunin, D.V.5    Grishin, E.V.6
  • 43
    • 0031910518 scopus 로고    scopus 로고
    • Characterisation of type-1 thionin loci from the A, B, D, and R genomes of wheat and rye
    • Van Campenhout S., Sagi L., Vander Stappen J., and Volckaert G. Characterisation of type-1 thionin loci from the A, B, D, and R genomes of wheat and rye. Theor. Appl. Genet. 96 (1998) 80-86
    • (1998) Theor. Appl. Genet. , vol.96 , pp. 80-86
    • Van Campenhout, S.1    Sagi, L.2    Vander Stappen, J.3    Volckaert, G.4
  • 44
    • 0029287210 scopus 로고
    • High conservation among sequences encoding type-V thionins in wheat and Aegilops
    • Castagnaro A., Segura A., and Garcia-Olmedo F. High conservation among sequences encoding type-V thionins in wheat and Aegilops. Plant Physiol 107 (1995) 1475-1476
    • (1995) Plant Physiol , vol.107 , pp. 1475-1476
    • Castagnaro, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 45
    • 0002849544 scopus 로고
    • Reallocation of the genomes of Triticum timopheevii Zhuk
    • Sears E.R., and Sears L.M.S. (Eds), University of Missouri, Columbia
    • Shands H., and Kimber G. Reallocation of the genomes of Triticum timopheevii Zhuk. In: Sears E.R., and Sears L.M.S. (Eds). Proc 4th Int Wheat Genet. Symp (1973), University of Missouri, Columbia 101-108
    • (1973) Proc 4th Int Wheat Genet. Symp , pp. 101-108
    • Shands, H.1    Kimber, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.