메뉴 건너뛰기




Volumn 403, Issue 1-2, 2007, Pages 29-38

Diverse forms of Pin-II family proteinase inhibitors from Capsicum annuum adversely affect the growth and development of Helicoverpa armigera

Author keywords

Insect resistance; IP repeats; PI insect interaction; Pichia pastoris; Potato type 2 inhibitors (Pot II); Solanaceae

Indexed keywords

CHYMOTRYPSIN; PROTEINASE INHIBITOR; PROTEINASE INHIBITOR PIN TYPE 2; UNCLASSIFIED DRUG;

EID: 34748903471     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.07.024     Document Type: Article
Times cited : (60)

References (37)
  • 2
    • 0034769603 scopus 로고    scopus 로고
    • Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annuum seeds
    • Antcheva N., et al. Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annuum seeds. Protein Sci. 10 (2001) 2280-2290
    • (2001) Protein Sci. , vol.10 , pp. 2280-2290
    • Antcheva, N.1
  • 3
    • 0027551083 scopus 로고
    • Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein, which is processed into five homologous inhibitors
    • Atkinson A.H., Heath R.L., Simpson R.J., Clarke A.E., and Anderson M.A. Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein, which is processed into five homologous inhibitors. Plant Cell 5 (1993) 203-213
    • (1993) Plant Cell , vol.5 , pp. 203-213
    • Atkinson, A.H.1    Heath, R.L.2    Simpson, R.J.3    Clarke, A.E.4    Anderson, M.A.5
  • 4
    • 0043234212 scopus 로고    scopus 로고
    • Unbound form of tomato inhibitor-II reveals inter-domain flexibility and conformational variability in the reactive site loops
    • Barrette-Ng I.H., et al. Unbound form of tomato inhibitor-II reveals inter-domain flexibility and conformational variability in the reactive site loops. J. Biol. Chem. 278 (2003) 31391-31400
    • (2003) J. Biol. Chem. , vol.278 , pp. 31391-31400
    • Barrette-Ng, I.H.1
  • 5
    • 0038267164 scopus 로고    scopus 로고
    • Structural basis of inhibition revealed by 1:2 complex of the two headed tomato inhibitor-II and subtilisin Carlsberg
    • Barrette-Ng I.H., Kenneth K.S.Ng., Cherney M.M., Pearce G., Ryan C.A., and James M.N.G. Structural basis of inhibition revealed by 1:2 complex of the two headed tomato inhibitor-II and subtilisin Carlsberg. J. Biol. Chem. 278 (2003) 24062-24071
    • (2003) J. Biol. Chem. , vol.278 , pp. 24062-24071
    • Barrette-Ng, I.H.1    Kenneth, K.S.Ng.2    Cherney, M.M.3    Pearce, G.4    Ryan, C.A.5    James, M.N.G.6
  • 6
    • 0036890373 scopus 로고    scopus 로고
    • Repeats with variations: accelerated evolution of the Pin2 family of proteinase inhibitors
    • Barta E., Pintar A., and Pongor S. Repeats with variations: accelerated evolution of the Pin2 family of proteinase inhibitors. Trends Genet. 18 (2002) 600-603
    • (2002) Trends Genet. , vol.18 , pp. 600-603
    • Barta, E.1    Pintar, A.2    Pongor, S.3
  • 7
    • 0034086003 scopus 로고    scopus 로고
    • Characterisation of potato proteinase inhibitor II reactive site mutants
    • Beekwilder J., Schipper B., Bakker P., Bosch D., and Jongsma M. Characterisation of potato proteinase inhibitor II reactive site mutants. Eur. J. Biochem. 267 (2000) 1975-1984
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1975-1984
    • Beekwilder, J.1    Schipper, B.2    Bakker, P.3    Bosch, D.4    Jongsma, M.5
  • 8
    • 0034697794 scopus 로고    scopus 로고
    • Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa
    • Choi D., Park J., Seo Y.S., Chun Y.J., and Kim W.T. Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa. Biochim. Biophys. Acta 1492 (2000) 211-215
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 211-215
    • Choi, D.1    Park, J.2    Seo, Y.S.3    Chun, Y.J.4    Kim, W.T.5
  • 10
    • 27744593837 scopus 로고    scopus 로고
    • Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)
    • Damle M.S., Giri A.P., Sainani M.N., and Gupta V.S. Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree). Phytochemistry 66 (2005) 2659-2667
    • (2005) Phytochemistry , vol.66 , pp. 2659-2667
    • Damle, M.S.1    Giri, A.P.2    Sainani, M.N.3    Gupta, V.S.4
  • 11
    • 0029670583 scopus 로고    scopus 로고
    • Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant
    • Duan X., Li X., Xue Q., Abo-El-Saad M., Xu D., and Wu R. Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant. Nat. Biotechnol. 14 (1996) 494-498
    • (1996) Nat. Biotechnol. , vol.14 , pp. 494-498
    • Duan, X.1    Li, X.2    Xue, Q.3    Abo-El-Saad, M.4    Xu, D.5    Wu, R.6
  • 14
    • 27744605309 scopus 로고    scopus 로고
    • Engineering insect tolerant plants using plant defensive proteinase inhibitors
    • Pandalai S.G. (Ed), Research Signpost, India
    • Giri A.P., Chougule N.P., Telang M.A., and Gupta V.S. Engineering insect tolerant plants using plant defensive proteinase inhibitors. In: Pandalai S.G. (Ed). Recent Research Developments in Phytochemistry 8 (2005), Research Signpost, India 117-137
    • (2005) Recent Research Developments in Phytochemistry , vol.8 , pp. 117-137
    • Giri, A.P.1    Chougule, N.P.2    Telang, M.A.3    Gupta, V.S.4
  • 15
    • 0001068883 scopus 로고
    • Wound induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects
    • Green T.R., and Ryan C.A. Wound induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects. Science 175 (1972) 776-777
    • (1972) Science , vol.175 , pp. 776-777
    • Green, T.R.1    Ryan, C.A.2
  • 16
    • 0032754118 scopus 로고    scopus 로고
    • Successive use of non-host plant proteinase inhibitors required for effective inhibition of gut proteinases and larval growth of Helicoverpa armigera
    • Harsulkar A.M., et al. Successive use of non-host plant proteinase inhibitors required for effective inhibition of gut proteinases and larval growth of Helicoverpa armigera. Plant Physiol. 121 (1999) 497-506
    • (1999) Plant Physiol. , vol.121 , pp. 497-506
    • Harsulkar, A.M.1
  • 17
    • 0029025551 scopus 로고
    • Characterization of the protease processing sites in a multidomain proteinase inhibitor precursor from Nicotiana alata
    • Heath R.L., Barton P.A., Simpson R.J., Reid G.E., Lim G., and Anderson M.A. Characterization of the protease processing sites in a multidomain proteinase inhibitor precursor from Nicotiana alata. Eur. J. Biochem. 230 (1995) 250-257
    • (1995) Eur. J. Biochem. , vol.230 , pp. 250-257
    • Heath, R.L.1    Barton, P.A.2    Simpson, R.J.3    Reid, G.E.4    Lim, G.5    Anderson, M.A.6
  • 18
    • 0031239547 scopus 로고    scopus 로고
    • Proteinase inhibitors from Nicotiana alata enhance plant resistance to insect pest
    • Heath R.L., et al. Proteinase inhibitors from Nicotiana alata enhance plant resistance to insect pest. J. Insect Physiol. 43 (1997) 833-842
    • (1997) J. Insect Physiol. , vol.43 , pp. 833-842
    • Heath, R.L.1
  • 19
    • 33644795085 scopus 로고    scopus 로고
    • Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuate
    • Horn M., et al. Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuate. Plant Physiol. 139 (2005) 375-388
    • (2005) Plant Physiol. , vol.139 , pp. 375-388
    • Horn, M.1
  • 20
    • 0024804111 scopus 로고
    • Expression of proteinase inhibitors I and II in transgenic plants: effects on natural defense against Manduca sexta larvae
    • Johnson R., Narvaez J., An G., and Ryan C.A. Expression of proteinase inhibitors I and II in transgenic plants: effects on natural defense against Manduca sexta larvae. Proc. Natl. Acad. Sci., USA 86 (1989) 9871-9875
    • (1989) Proc. Natl. Acad. Sci., USA , vol.86 , pp. 9871-9875
    • Johnson, R.1    Narvaez, J.2    An, G.3    Ryan, C.A.4
  • 21
    • 0029139370 scopus 로고
    • Phage display of a double-headed proteinase inhibitor: analysis of the binding domains of potato proteinase inhibitor II
    • Jongsma M.A., Bakker P.L., Stiekema W.J., and Bosch D. Phage display of a double-headed proteinase inhibitor: analysis of the binding domains of potato proteinase inhibitor II. Mol. Breed. 1 (1995) 181-191
    • (1995) Mol. Breed. , vol.1 , pp. 181-191
    • Jongsma, M.A.1    Bakker, P.L.2    Stiekema, W.J.3    Bosch, D.4
  • 22
    • 0034973578 scopus 로고    scopus 로고
    • Expression characteristics of serine proteinase inhibitor II under variable environmental stresses in hot pepper (Capsicum annuum L.)
    • Kim S., Hong Y., An C.S., and Lee K. Expression characteristics of serine proteinase inhibitor II under variable environmental stresses in hot pepper (Capsicum annuum L.). Plant Sci. 161 (2001) 27-33
    • (2001) Plant Sci. , vol.161 , pp. 27-33
    • Kim, S.1    Hong, Y.2    An, C.S.3    Lee, K.4
  • 23
    • 0033017462 scopus 로고    scopus 로고
    • A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein
    • Lee M.C.S., Scalon M.J., Craik D.J., and Anderson M.A. A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Nat. Struct. Biol. 6 (1999) 526-530
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 526-530
    • Lee, M.C.S.1    Scalon, M.J.2    Craik, D.J.3    Anderson, M.A.4
  • 24
    • 34748876355 scopus 로고    scopus 로고
    • Oviposition-stimulating activity of (E)-capsaicin identified in Capsicum annuum fruit and related compounds towards Helicoverpa assulta (Lepidoptera: Noctuidae)
    • Lee H., Hieu T.T., and Ahn Y. Oviposition-stimulating activity of (E)-capsaicin identified in Capsicum annuum fruit and related compounds towards Helicoverpa assulta (Lepidoptera: Noctuidae). Planta 226 (2007) 215-224
    • (2007) Planta , vol.226 , pp. 215-224
    • Lee, H.1    Hieu, T.T.2    Ahn, Y.3
  • 25
    • 0034006114 scopus 로고    scopus 로고
    • Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata
    • Miller E.A., Lee M.C., Atkinson A.H., and Anderson M.A. Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata. Plant Mol. Biol. 42 (2000) 329-333
    • (2000) Plant Mol. Biol. , vol.42 , pp. 329-333
    • Miller, E.A.1    Lee, M.C.2    Atkinson, A.H.3    Anderson, M.A.4
  • 26
    • 0034965916 scopus 로고    scopus 로고
    • Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin and methyl jasmonate
    • Moura D.S., and Ryan C.A. Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin and methyl jasmonate. Plant Physiol. 126 (2001) 289-298
    • (2001) Plant Physiol. , vol.126 , pp. 289-298
    • Moura, D.S.1    Ryan, C.A.2
  • 27
    • 0028823596 scopus 로고
    • Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata
    • Nielsen K.J., Heath R.L., Anderson M.A., and Craik D.J. Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata. Biochemistry 34 (1995) 14304-14311
    • (1995) Biochemistry , vol.34 , pp. 14304-14311
    • Nielsen, K.J.1    Heath, R.L.2    Anderson, M.A.3    Craik, D.J.4
  • 28
    • 0035103702 scopus 로고    scopus 로고
    • Complexity in specificities and expression of Helicoverpa armigera gut proteases explains polyphagous nature of the insect pest
    • Patankar A.G., et al. Complexity in specificities and expression of Helicoverpa armigera gut proteases explains polyphagous nature of the insect pest. Insect Biochem. Mol. Biol. 31 (2001) 453-464
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 453-464
    • Patankar, A.G.1
  • 29
    • 0033565476 scopus 로고    scopus 로고
    • Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata. Structure Fold
    • Scanlon M.J., Lee M.C., Anderson M.A., and Craik D.J. Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata. Structure Fold. Des. 7 (1999) 793-802
    • (1999) Des. , vol.7 , pp. 793-802
    • Scanlon, M.J.1    Lee, M.C.2    Anderson, M.A.3    Craik, D.J.4
  • 30
    • 21444454700 scopus 로고    scopus 로고
    • Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping
    • Schirra H.J., and Craik D.J. Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping. Prot. Peptide Letters 12 (2005) 421-431
    • (2005) Prot. Peptide Letters , vol.12 , pp. 421-431
    • Schirra, H.J.1    Craik, D.J.2
  • 31
    • 0034855725 scopus 로고    scopus 로고
    • Isolation of pepper mRNAs differentially expressed during the hypersensitive response to tobacco mosaic virus and characterization of a proteinase inhibitor gene
    • Shin R., et al. Isolation of pepper mRNAs differentially expressed during the hypersensitive response to tobacco mosaic virus and characterization of a proteinase inhibitor gene. Plant Sci. 161 (2001) 727-737
    • (2001) Plant Sci. , vol.161 , pp. 727-737
    • Shin, R.1
  • 32
    • 7044234943 scopus 로고    scopus 로고
    • Expression of proteinase inhibitor II proteins during floral development in Solanum americanum
    • Sin S.F., and Chye M.L. Expression of proteinase inhibitor II proteins during floral development in Solanum americanum. Planta 219 (2004) 1010-1022
    • (2004) Planta , vol.219 , pp. 1010-1022
    • Sin, S.F.1    Chye, M.L.2
  • 33
    • 33644852137 scopus 로고    scopus 로고
    • Down regulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development
    • Sin S., Yeung E.C., and Chye M. Down regulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development. Plant J. 45 (2006) 58-70
    • (2006) Plant J. , vol.45 , pp. 58-70
    • Sin, S.1    Yeung, E.C.2    Chye, M.3
  • 34
    • 17744371725 scopus 로고    scopus 로고
    • A Kunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on podborer (Helicoverpa armigera) larvae
    • Srinivasan A., Giri A.P., Harsulkar A.M., Gatehouse J.A., and Gupta V.S. A Kunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on podborer (Helicoverpa armigera) larvae. Plant Mol. Biol. 57 (2005) 359-374
    • (2005) Plant Mol. Biol. , vol.57 , pp. 359-374
    • Srinivasan, A.1    Giri, A.P.2    Harsulkar, A.M.3    Gatehouse, J.A.4    Gupta, V.S.5
  • 35
    • 14544285471 scopus 로고    scopus 로고
    • In vivo and in vitro effect of Capsicum annuum proteinase inhibitors on Helicoverpa armigera gut proteinases
    • Tamhane V.A., Chougule N.P., Giri A.P., Dixit A.R., Sainani M.N., and Gupta V.S. In vivo and in vitro effect of Capsicum annuum proteinase inhibitors on Helicoverpa armigera gut proteinases. Biochim. Biophys. Acta 1722 (2005) 156-167
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 156-167
    • Tamhane, V.A.1    Chougule, N.P.2    Giri, A.P.3    Dixit, A.R.4    Sainani, M.N.5    Gupta, V.S.6
  • 36
    • 1642506571 scopus 로고    scopus 로고
    • Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses
    • Zavala J.A., Patankar A.G., Gase K., Hui D., and Baldwin I.T. Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses. Plant Physiol. 134 (2004) 1181-1190
    • (2004) Plant Physiol. , vol.134 , pp. 1181-1190
    • Zavala, J.A.1    Patankar, A.G.2    Gase, K.3    Hui, D.4    Baldwin, I.T.5
  • 37
    • 34248583047 scopus 로고    scopus 로고
    • Larval feeding induced defensive responses in tobacco: comparison of two sibling species of Helicoverpa with divergent diet breadths
    • Zong N., and Wang C. Larval feeding induced defensive responses in tobacco: comparison of two sibling species of Helicoverpa with divergent diet breadths. Planta 226 (2007) 215-224
    • (2007) Planta , vol.226 , pp. 215-224
    • Zong, N.1    Wang, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.