메뉴 건너뛰기




Volumn 14, Issue 11, 2002, Pages 2863-2882

Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GENES; MASS SPECTROMETRY; POLYPEPTIDES; PROTEINS; SEED;

EID: 0036845735     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.005009     Document Type: Article
Times cited : (109)

References (52)
  • 2
    • 0028958785 scopus 로고
    • Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds
    • Becker, C., Shutov, A.D., Nong, V.H., Senyuk, V.I., Jung, R., Horstmann, C., Fischer, J., Nielsen, N.C., and Muntz, K. (1995). Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds. Eur. J. Biochem. 228, 456-462.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 456-462
    • Becker, C.1    Shutov, A.D.2    Nong, V.H.3    Senyuk, V.I.4    Jung, R.5    Horstmann, C.6    Fischer, J.7    Nielsen, N.C.8    Muntz, K.9
  • 3
    • 0025678423 scopus 로고
    • Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds
    • Belozersky, M.A., Dunaevsky, Y.E., and Voskoboynikova, N.E. (1990). Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds. Biochem. J. 272, 677-682.
    • (1990) Biochem. J. , vol.272 , pp. 677-682
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Voskoboynikova, N.E.3
  • 4
    • 0029827249 scopus 로고    scopus 로고
    • Yeast Gpi8p is essential for GPI anchor attachment onto proteins
    • Benghezal, M., Benachour, A., Rusconi, S., Aebi, M., and Conzelmann, A. (1996). Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J. 15, 6575-6583.
    • (1996) EMBO J. , vol.15 , pp. 6575-6583
    • Benghezal, M.1    Benachour, A.2    Rusconi, S.3    Aebi, M.4    Conzelmann, A.5
  • 5
    • 0034130561 scopus 로고    scopus 로고
    • Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays
    • Brenner, S., et al. (2000). Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays. Nat. Biotechnol. 18, 630-634.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 630-634
    • Brenner, S.1
  • 6
    • 0027508307 scopus 로고
    • An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro
    • D'Hondt, K., Bosch, D., Van Damme, J., Goethals, M., Vandekerckhove, J., and Krebbers, E. (1993). An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro. J. Biol. Chem. 268, 20884-20891.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20884-20891
    • D'Hondt, K.1    Bosch, D.2    Van Damme, J.3    Goethals, M.4    Vandekerckhove, J.5    Krebbers, E.6
  • 8
    • 0000990376 scopus 로고
    • Wheat seed carboxypeptidase and joint action on gliadin of proteases from dry and germinating seeds
    • Dunaevsky, Y.E., Sarbakanova, S.T., and Belozersky, M.A. (1989). Wheat seed carboxypeptidase and joint action on gliadin of proteases from dry and germinating seeds. J. Exp. Bot. 40, 1323-1329.
    • (1989) J. Exp. Bot. , vol.40 , pp. 1323-1329
    • Dunaevsky, Y.E.1    Sarbakanova, S.T.2    Belozersky, M.A.3
  • 9
    • 0033624194 scopus 로고    scopus 로고
    • The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: Developmental patterns, intracellular localization and functions in globulin proteolysis
    • Fischer, J., Becker, C., Hillmer, S., Horstmann, C., Neubohn, B., Schlereth, A., Senyuk, V., Shutov, A., and Muntz, K. (2000). The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: Developmental patterns, intracellular localization and functions in globulin proteolysis. Plant Mol. Biol. 43, 83-101.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 83-101
    • Fischer, J.1    Becker, C.2    Hillmer, S.3    Horstmann, C.4    Neubohn, B.5    Schlereth, A.6    Senyuk, V.7    Shutov, A.8    Muntz, K.9
  • 12
    • 0001842082 scopus 로고    scopus 로고
    • Asparaginyl endopeptidase
    • A. Barrett, N. Rawlings, and J. Woessner, eds (London: Academic Press)
    • Hara-Nishimura, I. (1998). Asparaginyl endopeptidase. In Handbook of Proteolytic Enzymes, A. Barrett, N. Rawlings, and J. Woessner, eds (London: Academic Press), pp. 746-749.
    • (1998) Handbook of Proteolytic Enzymes , pp. 746-749
    • Hara-Nishimura, I.1
  • 13
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura, I., Inoue, K., and Nishimura, M. (1991). A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett. 294, 89-93.
    • (1991) FEBS Lett. , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 14
    • 0027688051 scopus 로고
    • Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • Hara-Nishimura, I., Takeuchi, Y., and Nishimura, M. (1993). Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. Plant Cell 5, 1651-1659.
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 15
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 17
    • 0030993676 scopus 로고    scopus 로고
    • An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants
    • Hiraiwa, N., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (1997). An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants. Eur. J. Biochem. 246, 133-141.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 133-141
    • Hiraiwa, N.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 18
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants
    • Hoffman, L.M., Donaldson, D.D., and Herman, E.M. (1988). A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants. Plant Mol. Biol. 11, 717-729.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 717-729
    • Hoffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 19
    • 0028673279 scopus 로고
    • Legumain: Asparaginyl endopeptidase
    • Ishii, S. (1994). Legumain: Asparaginyl endopeptidase. Methods Enzymol. 244, 604-615.
    • (1994) Methods Enzymol. , vol.244 , pp. 604-615
    • Ishii, S.1
  • 21
    • 0000236658 scopus 로고
    • Site-specific limited proteolysis of legumin chloramphenicol acetyl transferase fusions in vitro and in transgenic tobacco seeds
    • Jung, R., Saalbach, G., Nielsen, N.C., and Muntz, K. (1993). Site-specific limited proteolysis of legumin chloramphenicol acetyl transferase fusions in vitro and in transgenic tobacco seeds. J. Exp. Bot. 44, 343-349.
    • (1993) J. Exp. Bot. , vol.44 , pp. 343-349
    • Jung, R.1    Saalbach, G.2    Nielsen, N.C.3    Muntz, K.4
  • 23
    • 0028815044 scopus 로고
    • Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco
    • Kermode, A.R., Fisher, S.A., Polishchuk, E., Wandelt, C., Spencer, D., and Higgins, T.J. (1995). Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco. Planta 197, 501-513.
    • (1995) Planta , vol.197 , pp. 501-513
    • Kermode, A.R.1    Fisher, S.A.2    Polishchuk, E.3    Wandelt, C.4    Spencer, D.5    Higgins, T.J.6
  • 24
    • 0029588601 scopus 로고
    • The sequence and expression of the gamma-VPE gene, one member of a family of three genes for vacuolar processing enzymes in Arabidopsis thaliana
    • Kinoshita, T., Nishimura, M., and Hara-Nishimura, I. (1995a). The sequence and expression of the gamma-VPE gene, one member of a family of three genes for vacuolar processing enzymes in Arabidopsis thaliana. Plant Cell Physiol. 36, 1555-1562.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1555-1562
    • Kinoshita, T.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 25
    • 0029379549 scopus 로고
    • Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana
    • Kinoshita, T., Nishimura, M., and Hara-Nishimura, I. (1995b). Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana. Plant Mol. Biol. 29, 81-89.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 81-89
    • Kinoshita, T.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 26
    • 0033166888 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions
    • Kinoshita, T., Yamada, K., Hiraiwa, N., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (1999). Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions. Plant J. 19, 43-53.
    • (1999) Plant J. , vol.19 , pp. 43-53
    • Kinoshita, T.1    Yamada, K.2    Hiraiwa, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 27
    • 0027274695 scopus 로고
    • Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana
    • Koizumi, M., Yamaguchi-Shinozaki, K., Tsuji, H., and Shinozaki, K. (1993). Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana. Gene 129, 175-182.
    • (1993) Gene , vol.129 , pp. 175-182
    • Koizumi, M.1    Yamaguchi-Shinozaki, K.2    Tsuji, H.3    Shinozaki, K.4
  • 29
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar, S., Tamura, K., Jakobsen, I.B., and Nei, M. (2001). MEGA2: Molecular evolutionary genetics analysis software. Bioinformatics 17, 1244-1245.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 30
    • 0036005912 scopus 로고    scopus 로고
    • Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide
    • Kuroyanagi, M., Nishimura, M., and Hara-Nishimura, I. (2002). Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide. Plant Cell Physiol. 43, 143-151.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 143-151
    • Kuroyanagi, M.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0032254026 scopus 로고    scopus 로고
    • Nucellain, a barley homolog of the dicot vacuolar-processing protease, is localized in nucellar cell walls
    • Linnestad, C., Doan, D.N., Brown, R.C., Lemmon, B.E., Meyer, D.J., Jung, R., and Olsen, O.A. (1998). Nucellain, a barley homolog of the dicot vacuolar-processing protease, is localized in nucellar cell walls. Plant Physiol. 118, 1169-1180.
    • (1998) Plant Physiol. , vol.118 , pp. 1169-1180
    • Linnestad, C.1    Doan, D.N.2    Brown, R.C.3    Lemmon, B.E.4    Meyer, D.J.5    Jung, R.6    Olsen, O.A.7
  • 34
    • 0000226387 scopus 로고
    • Seed development in Arabidopsis thaliana
    • E. Meyerowitz and C. Somerville, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Meinke, D. (1994). Seed development in Arabidopsis thaliana. In Arabidopsis, E. Meyerowitz and C. Somerville, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 253-295.
    • (1994) Arabidopsis , pp. 253-295
    • Meinke, D.1
  • 35
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Muntz, K. (1996). Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. J. Exp. Bot. 47, 605-622.
    • (1996) J. Exp. Bot. , vol.47 , pp. 605-622
    • Muntz, K.1
  • 36
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • Muntz, K. (1998). Deposition of storage proteins. Plant Mol. Biol. 38, 77-99.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 77-99
    • Muntz, K.1
  • 37
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Muntz, K., and Shutov, A. (2002). Legumains and their functions in plants. Trends Plant Sci. 7, 340-344.
    • (2002) Trends Plant Sci. , vol.7 , pp. 340-344
    • Muntz, K.1    Shutov, A.2
  • 38
    • 0028950917 scopus 로고
    • cDNA cloning for a putative cysteine proteinase from developing seeds of soybean
    • Nong, V.H., Becker, C., and Muntz, K. (1995). cDNA cloning for a putative cysteine proteinase from developing seeds of soybean. Biochim. Biophys. Acta 1261, 435-438.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 435-438
    • Nong, V.H.1    Becker, C.2    Muntz, K.3
  • 40
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and Lipman, D.J. (1988). Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 41
    • 0028894404 scopus 로고
    • Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole
    • Pueyo, J.J., Chrispeels, M.J., and Herman, E.M. (1995). Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta 196, 586-596.
    • (1995) Planta , vol.196 , pp. 586-596
    • Pueyo, J.J.1    Chrispeels, M.J.2    Herman, E.M.3
  • 42
    • 0028425479 scopus 로고
    • The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro
    • Runeberg-Roos, P., Kervinen, J., Kovaleva, V., Raikhel, N.V., and Gal, S. (1994). The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro. Plant Physiol. 105, 321-329.
    • (1994) Plant Physiol. , vol.105 , pp. 321-329
    • Runeberg-Roos, P.1    Kervinen, J.2    Kovaleva, V.3    Raikhel, N.V.4    Gal, S.5
  • 44
    • 0023472472 scopus 로고
    • Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. (1987). Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 45
    • 0035040254 scopus 로고    scopus 로고
    • Stored cysteine proteinases start globulin mobilization in protein bodies of embryonic axes and cotyledons during vetch (Vicia sativa L.) seed germination
    • Schlereth, A., Standhardt, D., Mock, H.P., and Muntz, K. (2001). Stored cysteine proteinases start globulin mobilization in protein bodies of embryonic axes and cotyledons during vetch (Vicia sativa L.) seed germination. Planta 212, 718-727.
    • (2001) Planta , vol.212 , pp. 718-727
    • Schlereth, A.1    Standhardt, D.2    Mock, H.P.3    Muntz, K.4
  • 46
    • 0026556773 scopus 로고
    • A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean
    • Scott, M.P., Jung, R., Muntz, K., and Nielsen, N.C. (1992). A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proc. Natl. Acad. Sci. USA 89, 658-662.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 658-662
    • Scott, M.P.1    Jung, R.2    Muntz, K.3    Nielsen, N.C.4
  • 47
    • 0028446555 scopus 로고
    • Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms
    • Shimada, T., Hiraiwa, N., Nishimura, M., and Hara-Nishimura, I. (1994). Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms. Plant Cell Physiol. 35, 713-718.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 713-718
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 48
    • 0025974129 scopus 로고
    • Characterization of the 12S globulin complex of Brassica napus: Evolutionary relationship to other 11-12S storage globulins
    • Sjodahl, S., Rodin, J., and Rask, L. (1991). Characterization of the 12S globulin complex of Brassica napus: Evolutionary relationship to other 11-12S storage globulins. Eur. J. Biochem. 196, 617-621.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 617-621
    • Sjodahl, S.1    Rodin, J.2    Rask, L.3
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). 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, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 0033213398 scopus 로고    scopus 로고
    • Multiple independent defective suppressor-mutator transposon insertions in Arabidopsis: A tool for functional genomics
    • Tissier, A.F., Marillonnet, S., Klimyuk, V., Patel, K., Torres, M.A., Murphy, G., and Jones, J.D. (1999). Multiple independent defective suppressor-mutator transposon insertions in Arabidopsis: A tool for functional genomics. Plant Cell 11, 1841-1852.
    • (1999) Plant Cell , vol.11 , pp. 1841-1852
    • Tissier, A.F.1    Marillonnet, S.2    Klimyuk, V.3    Patel, K.4    Torres, M.A.5    Murphy, G.6    Jones, J.D.7
  • 51
    • 0027573760 scopus 로고
    • A fifth 2S albumin isoform is present in Arabidopsis thaliana
    • van der Klei, H., Van Damme, J., Casteels, P., and Krebbers, E. (1993). A fifth 2S albumin isoform is present in Arabidopsis thaliana. Plant Physiol. 101, 1415-1416.
    • (1993) Plant Physiol. , vol.101 , pp. 1415-1416
    • Van der Klei, H.1    Van Damme, J.2    Casteels, P.3    Krebbers, E.4
  • 52
    • 0033593439 scopus 로고    scopus 로고
    • Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme
    • Yamada, K., Shimada, T., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (1999). Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme. J. Biol. Chem. 274, 2563-2570.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2563-2570
    • Yamada, K.1    Shimada, T.2    Kondo, M.3    Nishimura, M.4    Hara-Nishimura, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.