메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages 151-158

Arabidopsis F-box protein containing a Nictaba-related lectin domain interacts with N-acetyllactosamine structures

Author keywords

Carbohydrate binding; Fbs; Glycan array; LacNAc; Lewis structure; Nictaba; Plant lectin; Recombinant protein expression

Indexed keywords

ARABIDOPSIS PROTEIN; F BOX PROTEIN; GLYCAN; LECTIN; N ACETYLLACTOSAMINE SYNTHASE;

EID: 84863472557     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.06.002     Document Type: Article
Times cited : (29)

References (40)
  • 1
    • 0036616781 scopus 로고    scopus 로고
    • Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves
    • Chen Y., Peumans W.J., Hause B., Bras J., Kumar M., Proost P., Barre A., Rougé P., Van Damme E.J.M. Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves. FASEB J. 2002, 16:905-907.
    • (2002) FASEB J. , vol.16 , pp. 905-907
    • Chen, Y.1    Peumans, W.J.2    Hause, B.3    Bras, J.4    Kumar, M.5    Proost, P.6    Barre, A.7    Rougé, P.8    Van Damme, E.J.M.9
  • 4
    • 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
  • 5
    • 0001980363 scopus 로고
    • The isolation and some properties of a lectin (haemagglutinin) from Cucurbita phloem exudate
    • Sabnis D.D., Hart J.W. The isolation and some properties of a lectin (haemagglutinin) from Cucurbita phloem exudate. Planta 1978, 142:97-101.
    • (1978) Planta , vol.142 , pp. 97-101
    • Sabnis, D.D.1    Hart, J.W.2
  • 8
    • 0037143725 scopus 로고    scopus 로고
    • The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis
    • Gagne J.M., Downes B.P., Shiu S.H., Durski A.M., Vierstra R.D. The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc. Natl. Acad. Sci. USA 2002, 99:11519-11524.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11519-11524
    • Gagne, J.M.1    Downes, B.P.2    Shiu, S.H.3    Durski, A.M.4    Vierstra, R.D.5
  • 9
    • 53849102959 scopus 로고    scopus 로고
    • Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants?
    • Lannoo N., Peumans W.J., Van Damme E.J.M. Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants?. Biochem. Soc. Trans. 2008, 36:843-847.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 843-847
    • Lannoo, N.1    Peumans, W.J.2    Van Damme, E.J.M.3
  • 10
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.M., Elledge S.J. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 1996, 86:263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.M.6    Elledge, S.J.7
  • 11
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-ring ubiquitin ligases
    • Petroski M.D., Deshaies R.J. Function and regulation of cullin-ring ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2005, l6:9-20.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 13
    • 77949295782 scopus 로고    scopus 로고
    • Lectin-like ERAD players in ER and cytosol
    • Yoshida Y., Tanaka K. Lectin-like ERAD players in ER and cytosol. Biochim. Biophys. Acta 2010, 1800:172-180.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 172-180
    • Yoshida, Y.1    Tanaka, K.2
  • 15
    • 33751083838 scopus 로고    scopus 로고
    • Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans
    • Lannoo N., Peumans W.J., Van Pamel E., Alvarez R., Xiong T.-C., Hause G., Mazars C., Van Damme E.J.M. Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans. FEBS Lett. 2006, 580:6329-6337.
    • (2006) FEBS Lett. , vol.580 , pp. 6329-6337
    • Lannoo, N.1    Peumans, W.J.2    Van Pamel, E.3    Alvarez, R.4    Xiong, T.-C.5    Hause, G.6    Mazars, C.7    Van Damme, E.J.M.8
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 62849091082 scopus 로고    scopus 로고
    • Structures common to different glycans
    • Cold Spring Harbor Laboratory Press, NY, Chapter 13, A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.)
    • Stanley P., Cummings R.D. Structures common to different glycans. Essentials of Glycobiology 2009, 175-198. Cold Spring Harbor Laboratory Press, NY, Chapter 13. 2nd ed. A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.).
    • (2009) Essentials of Glycobiology , pp. 175-198
    • Stanley, P.1    Cummings, R.D.2
  • 22
    • 0033948727 scopus 로고    scopus 로고
    • Lewis antigens in Helicobacter pylori: biosynthesis and phase variation
    • Wang G., Ge Z., Rasko D.A., Taylor D.E. Lewis antigens in Helicobacter pylori: biosynthesis and phase variation. Mol. Microbiol. 2000, 36:1187-1196.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1187-1196
    • Wang, G.1    Ge, Z.2    Rasko, D.A.3    Taylor, D.E.4
  • 26
    • 0031590175 scopus 로고    scopus 로고
    • a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vacciniummyrtillus L.)
    • a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vacciniummyrtillus L.). FEBS Lett. 1997, 415:186-191.
    • (1997) FEBS Lett. , vol.415 , pp. 186-191
    • Melo, N.S.1    Nimtz, M.2    Conradt, H.S.3    Fevereiro, P.S.4    Costa, J.5
  • 28
    • 0034958453 scopus 로고    scopus 로고
    • Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core α1,3-linked fucose and xylose substitutions
    • Wilson I.B., Zeleny R., Kolarich D., Staudacher E., Stroop C.J., Kamerling J.P., Altmann F. Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core α1,3-linked fucose and xylose substitutions. Glycobiology 2001, 11:261-274.
    • (2001) Glycobiology , vol.11 , pp. 261-274
    • Wilson, I.B.1    Zeleny, R.2    Kolarich, D.3    Staudacher, E.4    Stroop, C.J.5    Kamerling, J.P.6    Altmann, F.7
  • 33
    • 77249131695 scopus 로고    scopus 로고
    • Reduction of N-linked xylose and fucose by expression of rat β1,4-N-acetylglucosaminyltransferase III in tobacco BY-2 cells depends on Golgi enzyme localization domain and genetic elements used for expression
    • Karg S.R., Frey A.D., Kallio P.T. Reduction of N-linked xylose and fucose by expression of rat β1,4-N-acetylglucosaminyltransferase III in tobacco BY-2 cells depends on Golgi enzyme localization domain and genetic elements used for expression. J. Biotechnol. 2010, 146:54-65.
    • (2010) J. Biotechnol. , vol.146 , pp. 54-65
    • Karg, S.R.1    Frey, A.D.2    Kallio, P.T.3
  • 34
    • 16844369621 scopus 로고    scopus 로고
    • Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates
    • Yoshida Y., Adachi E., Fukiya K., Iwai K., Tanaka K. Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates. EMBO Rep. 2005, 6:239-244.
    • (2005) EMBO Rep. , vol.6 , pp. 239-244
    • Yoshida, Y.1    Adachi, E.2    Fukiya, K.3    Iwai, K.4    Tanaka, K.5
  • 35
    • 45149112519 scopus 로고    scopus 로고
    • Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases
    • Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L. Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases. J. Biol. Chem. 2008, 283:12717-12729.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12717-12729
    • Glenn, K.A.1    Nelson, R.F.2    Wen, H.M.3    Mallinger, A.J.4    Paulson, H.L.5
  • 36
    • 84867334754 scopus 로고    scopus 로고
    • Functional characterization of a jasmonate-inducible carbohydrate-binding protein in tobacco plants. PhD thesis, Ghent University
    • Lannoo, N., 2007. Functional characterization of a jasmonate-inducible carbohydrate-binding protein in tobacco plants. PhD thesis, Ghent University, p. 253.
    • (2007) , pp. 253
    • Lannoo, N.1
  • 38
    • 0345269215 scopus 로고    scopus 로고
    • A structural basis for the difference in specificity between the two jacalin-related lectins from mulberry (Morusnigra) bark
    • Rougé P., Peumans W.J., Barre A., Van Damme E.J.M. A structural basis for the difference in specificity between the two jacalin-related lectins from mulberry (Morusnigra) bark. Biochem. Biophys. Res. Commun. 2003, 304:91-97.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 91-97
    • Rougé, P.1    Peumans, W.J.2    Barre, A.3    Van Damme, E.J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.