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Volumn 580, Issue 25, 2006, Pages 5822-5828

Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus

Author keywords

Capsid protein; O glycosylation; Plum pox virus; Potyvirus

Indexed keywords

AMINO ACID; CAPSID PROTEIN; MONOMER; N ACETYLGLUCOSAMINE; THREONINE;

EID: 33750058261     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.09.041     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0030725323 scopus 로고    scopus 로고
    • Post-translational modification of proteins and the discovery of new medicine
    • Parekh R.B., and Rohlff C. Post-translational modification of proteins and the discovery of new medicine. Curr. Opin. Biotechnol. 8 (1997) 718-723
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 718-723
    • Parekh, R.B.1    Rohlff, C.2
  • 2
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro R.G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12 (2002) 43R-56R
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 3
    • 33750047818 scopus 로고    scopus 로고
    • Cytoplasmic glycosylation
    • (Editorial)
    • Hart G.W. Cytoplasmic glycosylation. Biochim. Biophys. Acta 1673 (2004) 1 (Editorial)
    • (2004) Biochim. Biophys. Acta , vol.1673 , pp. 1
    • Hart, G.W.1
  • 4
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells L., Vosseller K., and Hart G.W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291 (2001) 2376-2378
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 5
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • Shafi R., Iyer S.P., Ellies L.G., O'Donnell N., Marek K.W., Chui D., Hart G.W., and Marth J.D. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc. Natl. Acad. Sci. USA 97 (2000) 5735-5739
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6    Hart, G.W.7    Marth, J.D.8
  • 6
    • 30044438532 scopus 로고    scopus 로고
    • O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks
    • Slawson C., Housley M.P., and Hart G.W. O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks. J. Cell. Biochem. 97 (2006) 71-83
    • (2006) J. Cell. Biochem. , vol.97 , pp. 71-83
    • Slawson, C.1    Housley, M.P.2    Hart, G.W.3
  • 7
    • 0036898933 scopus 로고    scopus 로고
    • Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification
    • Vosseller K., Sakabe K., Wells L., and Hart G.W. Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification. Curr. Opin. Chem. Biol. 6 (2002) 851-857
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 851-857
    • Vosseller, K.1    Sakabe, K.2    Wells, L.3    Hart, G.W.4
  • 8
    • 4644262462 scopus 로고    scopus 로고
    • O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
    • Wells L., Kreppel L.K., Comer F.I., Wadzinski B.E., and Hart G.W. O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits. J. Biol. Chem. 279 (2004) 38466-38470
    • (2004) J. Biol. Chem. , vol.279 , pp. 38466-38470
    • Wells, L.1    Kreppel, L.K.2    Comer, F.I.3    Wadzinski, B.E.4    Hart, G.W.5
  • 9
    • 0036021405 scopus 로고    scopus 로고
    • Two O-Linked N-Acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development
    • Hartweck L.M., Scott C.L., and Olszewski N.E. Two O-Linked N-Acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development. Genetics 161 (2002) 1279-1291
    • (2002) Genetics , vol.161 , pp. 1279-1291
    • Hartweck, L.M.1    Scott, C.L.2    Olszewski, N.E.3
  • 10
    • 0000519058 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of Arabidopsis SPY
    • Altman A., Ziv M., and Izhar S. (Eds), Kluwer Academic Publishers., Dordrecht, The Netherlands
    • Thornton T.M., Kreppel L., Hart G.W., and Olszewski N.E. Genetic and biochemical analysis of Arabidopsis SPY. In: Altman A., Ziv M., and Izhar S. (Eds). Plant Biotechnology and In Vitro Biology in the 21st Century (1999), Kluwer Academic Publishers., Dordrecht, The Netherlands 445-448
    • (1999) Plant Biotechnology and In Vitro Biology in the 21st Century , pp. 445-448
    • Thornton, T.M.1    Kreppel, L.2    Hart, G.W.3    Olszewski, N.E.4
  • 11
    • 0032051572 scopus 로고    scopus 로고
    • A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases
    • Heese-Peck A., and Raikhel N.V. A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases. Plant Cell 10 (1998) 599-612
    • (1998) Plant Cell , vol.10 , pp. 599-612
    • Heese-Peck, A.1    Raikhel, N.V.2
  • 12
    • 0029360464 scopus 로고
    • Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine
    • Heese-Peck A., Cole R.N., Borkhsenious O.N., Hart G.W., and Raikhel N.V. Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. Plant Cell 7 (1995) 1459-1471
    • (1995) Plant Cell , vol.7 , pp. 1459-1471
    • Heese-Peck, A.1    Cole, R.N.2    Borkhsenious, O.N.3    Hart, G.W.4    Raikhel, N.V.5
  • 14
    • 33644922089 scopus 로고    scopus 로고
    • SECRET AGENT and SPINDLY have overlapping roles in the development of Arabidopsis thaliana L. Heyn
    • Hartweck L.M., Genger R.K., Grey W.M., and Olszewski N.E. SECRET AGENT and SPINDLY have overlapping roles in the development of Arabidopsis thaliana L. Heyn. J. Exp. Bot. 57 (2006) 865-875
    • (2006) J. Exp. Bot. , vol.57 , pp. 865-875
    • Hartweck, L.M.1    Genger, R.K.2    Grey, W.M.3    Olszewski, N.E.4
  • 16
    • 33751006999 scopus 로고    scopus 로고
    • Scott, C.L., Hartweck, L.M., Pérez, J.J., Chen, D., García, J.A. and Olszewski, N.E. (2006) SECRET AGENT, an Arabidopsis thaliana O-GlcNAc transferase, modifies the Plum pox virus capsid protein. FEBS Lett. 580, this issue, doi:10.1016/j.febslet.2006.09.046.
  • 18
    • 0032949311 scopus 로고    scopus 로고
    • New advances in understanding the molecular biology of plant/potyvirus interactions
    • Revers F., Le Gall O., Candresse T., and Maule A.J. New advances in understanding the molecular biology of plant/potyvirus interactions. Mol. Plant-Microbe Interact. 12 (1999) 367-376
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 367-376
    • Revers, F.1    Le Gall, O.2    Candresse, T.3    Maule, A.J.4
  • 19
    • 0026573174 scopus 로고
    • Highlights and prospects of potyvirus molecular biology
    • Riechmann J.L., Laín S., and García J.A. Highlights and prospects of potyvirus molecular biology. J. Gen. Virol. 73 (1992) 1-16
    • (1992) J. Gen. Virol. , vol.73 , pp. 1-16
    • Riechmann, J.L.1    Laín, S.2    García, J.A.3
  • 20
    • 0034631736 scopus 로고    scopus 로고
    • Construction of a stable and highly infectious intron-containing cDNA clone of plum pox potyvirus and its use to infect plants by particle bombardment
    • López-Moya J.J., and García J.A. Construction of a stable and highly infectious intron-containing cDNA clone of plum pox potyvirus and its use to infect plants by particle bombardment. Virus Res. 68 (2000) 99-107
    • (2000) Virus Res. , vol.68 , pp. 99-107
    • López-Moya, J.J.1    García, J.A.2
  • 21
    • 0000624742 scopus 로고
    • Nucleotide sequence of the 3′ terminal region of plum pox potyvirus RNA
    • Laín S., Riechmann J.L., Méndez E., and García J.A. Nucleotide sequence of the 3′ terminal region of plum pox potyvirus RNA. Virus Res. 10 (1988) 325-342
    • (1988) Virus Res. , vol.10 , pp. 325-342
    • Laín, S.1    Riechmann, J.L.2    Méndez, E.3    García, J.A.4
  • 22
    • 0035866318 scopus 로고    scopus 로고
    • Protection of rabbits against rabbit hemorrhagic disease virus by immunization with the VP60 protein expressed in plants with a potyvirus-based vector
    • Fernández-Fernández M.R., Mouriño M., Rivera J., Rodríguez F., Plana-Durán J., and García J.A. Protection of rabbits against rabbit hemorrhagic disease virus by immunization with the VP60 protein expressed in plants with a potyvirus-based vector. Virology 280 (2001) 283-291
    • (2001) Virology , vol.280 , pp. 283-291
    • Fernández-Fernández, M.R.1    Mouriño, M.2    Rivera, J.3    Rodríguez, F.4    Plana-Durán, J.5    García, J.A.6
  • 23
    • 0029311267 scopus 로고
    • Jellyfish green fluorescent protein as a reporter for virus infections
    • Baulcombe D., Chapman S., and Santa Cruz S. Jellyfish green fluorescent protein as a reporter for virus infections. Plant J. 7 (1995) 1045-1053
    • (1995) Plant J. , vol.7 , pp. 1045-1053
    • Baulcombe, D.1    Chapman, S.2    Santa Cruz, S.3
  • 24
    • 0025063721 scopus 로고
    • A general and rapid mutagenesis method using polymerase chain reaction
    • Herlitze S., and Koenen M. A general and rapid mutagenesis method using polymerase chain reaction. Gene 91 (1990) 143-147
    • (1990) Gene , vol.91 , pp. 143-147
    • Herlitze, S.1    Koenen, M.2
  • 25
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66 (1997) 315-335
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 26
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., and Hart G.W. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cel. Proteomics 1 (2002) 791-804
    • (2002) Mol. Cel. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 28
    • 0029122424 scopus 로고
    • Transmission by aphids of a naturally non-transmissible plum pox virus isolate with the aid of potato virus Y helper component
    • López-Moya J.J., Canto T., Díaz-Ruíz J.R., and López-Abella D. Transmission by aphids of a naturally non-transmissible plum pox virus isolate with the aid of potato virus Y helper component. J. Gen. Virol. 76 (1995) 2293-2297
    • (1995) J. Gen. Virol. , vol.76 , pp. 2293-2297
    • López-Moya, J.J.1    Canto, T.2    Díaz-Ruíz, J.R.3    López-Abella, D.4
  • 29
    • 33144462048 scopus 로고    scopus 로고
    • Distinct viral populations differentiate and evolve independently in a single perennial host plant
    • Jridi C., Martin J.F., Marie-Jeanne V., Labonne G., and Blanc S. Distinct viral populations differentiate and evolve independently in a single perennial host plant. J. Virol. 80 (2006) 2349-2357
    • (2006) J. Virol. , vol.80 , pp. 2349-2357
    • Jridi, C.1    Martin, J.F.2    Marie-Jeanne, V.3    Labonne, G.4    Blanc, S.5
  • 30
    • 33646012646 scopus 로고    scopus 로고
    • Glycosylation of beet western yellows virus proteins is implicated in the aphid transmission of the virus
    • Seddas P., and Boissinot S. Glycosylation of beet western yellows virus proteins is implicated in the aphid transmission of the virus. Arch. Virol. 151 (2005) 967-984
    • (2005) Arch. Virol. , vol.151 , pp. 967-984
    • Seddas, P.1    Boissinot, S.2
  • 31
    • 0025810911 scopus 로고
    • Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine
    • Gonzalez S.A., and Burrone O.R. Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine. Virology 182 (1991) 8-16
    • (1991) Virology , vol.182 , pp. 8-16
    • Gonzalez, S.A.1    Burrone, O.R.2
  • 32
    • 0028138572 scopus 로고
    • Site-specific glycosylation of the human cytomegalovirus tegument basic phosphoprotein (UL32) at serine 921 and serine 952
    • Greis K.D., Gibson W., and Hart G.W. Site-specific glycosylation of the human cytomegalovirus tegument basic phosphoprotein (UL32) at serine 921 and serine 952. J. Virol. 68 (1994) 8339-8849
    • (1994) J. Virol. , vol.68 , pp. 8339-8849
    • Greis, K.D.1    Gibson, W.2    Hart, G.W.3
  • 33
    • 0025007072 scopus 로고
    • Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins
    • Mullis K.G., Haltiwanger R.S., Hart G.W., Marchase R.B., and Engler J.A. Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins. J. Virol. 64 (1990) 5317-5323
    • (1990) J. Virol. , vol.64 , pp. 5317-5323
    • Mullis, K.G.1    Haltiwanger, R.S.2    Hart, G.W.3    Marchase, R.B.4    Engler, J.A.5
  • 34
    • 0026736507 scopus 로고
    • A structural polypeptide of the baculovirus Autographa californica nuclear polyhedrosis virus contains O-linked N-acetylglucosamine
    • Whitford M., and Faulkner P. A structural polypeptide of the baculovirus Autographa californica nuclear polyhedrosis virus contains O-linked N-acetylglucosamine. J. Virol. 66 (1992) 3324-3329
    • (1992) J. Virol. , vol.66 , pp. 3324-3329
    • Whitford, M.1    Faulkner, P.2
  • 35
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor β
    • Cheng X., Cole R.N., Zaia J., and Hart G.W. Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor β. Biochemistry 39 (2000) 11609-11620
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 36
    • 0141884304 scopus 로고    scopus 로고
    • Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation
    • Slawson C., and Hart G.W. Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation. Curr. Opin. Struct. Biol. 13 (2003) 631-636
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 631-636
    • Slawson, C.1    Hart, G.W.2
  • 38
    • 0035957981 scopus 로고    scopus 로고
    • Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A
    • Ivanov K.I., Puustinen P., Merits A., Saarma M., and Mäkinen K. Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A. J. Biol. Chem. 276 (2001) 13530-13540
    • (2001) J. Biol. Chem. , vol.276 , pp. 13530-13540
    • Ivanov, K.I.1    Puustinen, P.2    Merits, A.3    Saarma, M.4    Mäkinen, K.5
  • 39
    • 0034990528 scopus 로고    scopus 로고
    • A nonviral peptide can replace the entire N terminus of zucchini yellow mosaic potyvirus coat protein and permits viral systemic infection
    • Arazi T., Shiboleth Y.M., and Gal-On A. A nonviral peptide can replace the entire N terminus of zucchini yellow mosaic potyvirus coat protein and permits viral systemic infection. J. Virol. 75 (2001) 6329-6336
    • (2001) J. Virol. , vol.75 , pp. 6329-6336
    • Arazi, T.1    Shiboleth, Y.M.2    Gal-On, A.3
  • 40
    • 7444222984 scopus 로고    scopus 로고
    • Maintenance of coat protein N-terminal net charge and not primary sequence is essential for zucchini yellow mosaic virus systemic infectivity
    • Kimalov B., Gal-On A., Stav R., Belausov E., and Arazi T. Maintenance of coat protein N-terminal net charge and not primary sequence is essential for zucchini yellow mosaic virus systemic infectivity. J. Gen. Virol. 85 (2004) 3421-3430
    • (2004) J. Gen. Virol. , vol.85 , pp. 3421-3430
    • Kimalov, B.1    Gal-On, A.2    Stav, R.3    Belausov, E.4    Arazi, T.5
  • 41
    • 0031974475 scopus 로고    scopus 로고
    • Charge changes near the N terminus of the coat protein of two potyviruses affect virus movement
    • López-Moya J.J., and Pirone T.P. Charge changes near the N terminus of the coat protein of two potyviruses affect virus movement. J. Gen. Virol. 79 (1998) 161-165
    • (1998) J. Gen. Virol. , vol.79 , pp. 161-165
    • López-Moya, J.J.1    Pirone, T.P.2


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