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Volumn 443, Issue 1, 2014, Pages 18-21

Molecular chaperone function of Arabidopsis thaliana phloem protein 2-A1, encodes a protein similar to phloem lectin

Author keywords

Antifungal activity; Arabidopsis thaliana; Lectin; Molecular chaperone; Phloem protein

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; ETHYLENE; JASMONIC ACID; MALATE DEHYDROGENASE; PHLOEM LECTIN; PHLOEM PROTEIN 2 A1; PLANT LECTIN; RECOMBINANT PROTEIN; SALICYLIC ACID; SIGNALING LYMPHOCYTE ACTIVATION MOLECULE ASSOCIATED PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 84890856499     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.11.034     Document Type: Article
Times cited : (27)

References (26)
  • 1
    • 33745954371 scopus 로고    scopus 로고
    • Integrative plant biology: role of phloem long-distance macromolecular trafficking
    • Lough T.J., Lucas W.J. Integrative plant biology: role of phloem long-distance macromolecular trafficking. Annu. Rev. Plant Biol. 2006, 57:203-232.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 203-232
    • Lough, T.J.1    Lucas, W.J.2
  • 2
    • 4544353843 scopus 로고    scopus 로고
    • Pathogen-induced resistance and alarm signals in the phloem
    • VAN Bel A.J., Gaupels F. Pathogen-induced resistance and alarm signals in the phloem. Mol. Plant Pathol. 2004, 5:495-504.
    • (2004) Mol. Plant Pathol. , vol.5 , pp. 495-504
    • Van Bel, A.J.1    Gaupels, F.2
  • 5
    • 33644926728 scopus 로고    scopus 로고
    • Phloem sap proteins: their identities and potential roles in the interaction between plants and phloem-feeding insects
    • Kehr J. Phloem sap proteins: their identities and potential roles in the interaction between plants and phloem-feeding insects. J. Exp. Bot. 2006, 57:767-774.
    • (2006) J. Exp. Bot. , vol.57 , pp. 767-774
    • Kehr, J.1
  • 6
    • 0021104639 scopus 로고
    • Subunit structure and interactions of the phloem proteins of Cucurbita maxima (Pumpkin)
    • Read S.M., Northcote D.H. Subunit structure and interactions of the phloem proteins of Cucurbita maxima (Pumpkin). Eur. J. Biochem. 1983, 134:561-569.
    • (1983) Eur. J. Biochem. , vol.134 , pp. 561-569
    • Read, S.M.1    Northcote, D.H.2
  • 7
    • 33644890500 scopus 로고    scopus 로고
    • Physical and chemical interactions between aphids and plants
    • Will T., van Bel A.J. Physical and chemical interactions between aphids and plants. J. Exp. Bot. 2006, 57:729-737.
    • (2006) J. Exp. Bot. , vol.57 , pp. 729-737
    • Will, T.1    van Bel, A.J.2
  • 8
    • 33644929267 scopus 로고    scopus 로고
    • Salivary secretions by aphids interacting with proteins of phloem wound responses
    • Tjallingii W.F. Salivary secretions by aphids interacting with proteins of phloem wound responses. J. Exp. Bot. 2006, 57:739-745.
    • (2006) J. Exp. Bot. , vol.57 , pp. 739-745
    • Tjallingii, W.F.1
  • 9
    • 78651303570 scopus 로고    scopus 로고
    • Harpin-induced expression and transgenic overexpression of the phloem protein gene AtPP2-A1 in Arabidopsis repress phloem feeding of the green peach aphid Myzus persicae
    • Zhang C., Shi H., Chen L., Wang X., Lu B., Zhang S., Liang Y., Liu R., Qian J., Sun W., You Z., Dong H. Harpin-induced expression and transgenic overexpression of the phloem protein gene AtPP2-A1 in Arabidopsis repress phloem feeding of the green peach aphid Myzus persicae. BMC Plant Biol. 2011, 11:11.
    • (2011) BMC Plant Biol. , vol.11 , pp. 11
    • Zhang, C.1    Shi, H.2    Chen, L.3    Wang, X.4    Lu, B.5    Zhang, S.6    Liang, Y.7    Liu, R.8    Qian, J.9    Sun, W.10    You, Z.11    Dong, H.12
  • 10
    • 33749262455 scopus 로고    scopus 로고
    • The internal glycine-rich motif and cysteine suppress several effects of the HpaG(Xooc) protein in plants
    • Liu F., Liu H., Jia Q., Wu X., Guo X., Zhang S., Song F., Dong H. The internal glycine-rich motif and cysteine suppress several effects of the HpaG(Xooc) protein in plants. Phytopathology 2006, 96:1052-1059.
    • (2006) Phytopathology , vol.96 , pp. 1052-1059
    • Liu, F.1    Liu, H.2    Jia, Q.3    Wu, X.4    Guo, X.5    Zhang, S.6    Song, F.7    Dong, H.8
  • 11
    • 4644371409 scopus 로고    scopus 로고
    • Expression of harpin(xoo) in transgenic tobacco induces pathogen defense in the absence of hypersensitive cell death
    • Peng J.L., Bao Z.L., Ren H.Y., Wang J.S., Dong H.S. Expression of harpin(xoo) in transgenic tobacco induces pathogen defense in the absence of hypersensitive cell death. Phytopathology 2004, 94:1048-1055.
    • (2004) Phytopathology , vol.94 , pp. 1048-1055
    • Peng, J.L.1    Bao, Z.L.2    Ren, H.Y.3    Wang, J.S.4    Dong, H.S.5
  • 13
    • 33644884491 scopus 로고    scopus 로고
    • Transcriptomics and functional genomics of plant defence induction by phloem-feeding insects
    • Thompson G.A., Goggin F.L. Transcriptomics and functional genomics of plant defence induction by phloem-feeding insects. J. Exp. Bot. 2006, 57:755-766.
    • (2006) J. Exp. Bot. , vol.57 , pp. 755-766
    • Thompson, G.A.1    Goggin, F.L.2
  • 14
    • 54549123443 scopus 로고    scopus 로고
    • Functional characterization of pathogen-responsive protein AtDabb1 with an antifungal activity from Arabidopsis thaliana
    • Lee J.R., Lee S.S., Park S.C., Kang J.S., Kim S.Y., Lee K.O., Lee S.Y. Functional characterization of pathogen-responsive protein AtDabb1 with an antifungal activity from Arabidopsis thaliana. Biochim. Biophys. Acta 2008, 1784:1918-1923.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1918-1923
    • Lee, J.R.1    Lee, S.S.2    Park, S.C.3    Kang, J.S.4    Kim, S.Y.5    Lee, K.O.6    Lee, S.Y.7
  • 15
    • 0342444416 scopus 로고
    • GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson R.A., Kavanagh T.A., Bevan M.W. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 1987, 6:3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 16
    • 33845435000 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method
    • Zhang X., Henriques R., Lin S.S., Niu Q.W., Chua N.H. Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method. Nat. Protoc. 2006, 1:641-646.
    • (2006) Nat. Protoc. , vol.1 , pp. 641-646
    • Zhang, X.1    Henriques, R.2    Lin, S.S.3    Niu, Q.W.4    Chua, N.H.5
  • 20
    • 4644313922 scopus 로고    scopus 로고
    • A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization
    • Haslbeck M., Ignatiou A., Saibil H., Helmich S., Frenzl E., Stromer T., Buchner J. A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J. Mol. Biol. 2004, 343:445-455.
    • (2004) J. Mol. Biol. , vol.343 , pp. 445-455
    • Haslbeck, M.1    Ignatiou, A.2    Saibil, H.3    Helmich, S.4    Frenzl, E.5    Stromer, T.6    Buchner, J.7
  • 21
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman B., Ramakrishna T., Rao C.M. Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 1995, 365:133-136.
    • (1995) FEBS Lett. , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 22
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of alpha-crystallin
    • Raman B., Rao C.M. Chaperone-like activity and temperature-induced structural changes of alpha-crystallin. J. Biol. Chem. 1997, 272:23559-23564.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23559-23564
    • Raman, B.1    Rao, C.M.2
  • 23
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G.J., Roseman A.M., Saibil H.R., Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 1997, 16:659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.