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Volumn 46, Issue 1, 2005, Pages 87-98

The rice nucellin gene ortholog OsAsp1 encodes an active aspartic protease without a plant-specific insert and is strongly expressed in early embryo

Author keywords

Aspartic protease; Embryo; Gene expression; Recombinant protein; Rice (Oryza sativa L.)

Indexed keywords

ASPARTIC PROTEINASE; MESSENGER RNA; NUCELLIN; PLANT DNA; PLANT RNA; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 14644393639     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/pci002     Document Type: Article
Times cited : (37)

References (44)
  • 1
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408: 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 2
    • 0033869219 scopus 로고    scopus 로고
    • The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin
    • Asakura, T., Matsumoto, I., Funaki, J., Arai, S. and Abe, K. (2000) The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin. Eur. J. Biochem. 267: 5115-5122.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5115-5122
    • Asakura, T.1    Matsumoto, I.2    Funaki, J.3    Arai, S.4    Abe, K.5
  • 3
    • 0029101380 scopus 로고
    • Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases
    • Asakura, T., Watanabe, H., Abe, K. and Arai, S. (1995) Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases. Eur. J. Biochem. 232: 77-83.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 77-83
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 4
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: Possible roles during programmed cell death
    • Beers, E.P., Woffenden, B.J. and Zhao, C.S. (2000) Plant proteolytic enzymes: possible roles during programmed cell death. Plant Mol. Biol. 44: 399-415.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.S.3
  • 5
    • 0031457314 scopus 로고    scopus 로고
    • Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration
    • Chen, F. and Foolad, M.R. (1997) Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration. Plant Mol. Biol. 35: 821-831.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 821-831
    • Chen, F.1    Foolad, M.R.2
  • 6
    • 0033055250 scopus 로고    scopus 로고
    • Nucellar-cell-specific expression of a lipid transfer protein gene in barley (Hordeum vulgare L.)
    • Chen, F., and Foolad, M.R. (1999) Nucellar-cell-specific expression of a lipid transfer protein gene in barley (Hordeum vulgare L.). Plant Cell Rep. 18: 445-450.
    • (1999) Plant Cell Rep. , vol.18 , pp. 445-450
    • Chen, F.1    Foolad, M.R.2
  • 7
    • 0033004659 scopus 로고    scopus 로고
    • Isolation and characterization of a gene expressed during early embryo sac development in apomictic guinea grass (Panicum maximum)
    • Chen, L.Z., Miyazaki, C., Kojima, A., Saito, A. and Adachi, T. (1999) Isolation and characterization of a gene expressed during early embryo sac development in apomictic guinea grass (Panicum maximum). J. Plant Physiol. 154: 55-62.
    • (1999) J. Plant Physiol. , vol.154 , pp. 55-62
    • Chen, L.Z.1    Miyazaki, C.2    Kojima, A.3    Saito, A.4    Adachi, T.5
  • 8
    • 0027527056 scopus 로고
    • RNA-RNA in situ hybridization using digoxigenin-labeled probes, the use of high molecular weight polyvinyl alcohol in the alkaline phosphatase indoxyl-nitroblue tetrazolium
    • DeBlock, M. and Debrouwer, D. (1993) RNA-RNA in situ hybridization using digoxigenin-labeled probes, the use of high molecular weight polyvinyl alcohol in the alkaline phosphatase indoxyl-nitroblue tetrazolium. Anal. Biochem. 216: 88-89
    • (1993) Anal. Biochem. , vol.216 , pp. 88-89
    • DeBlock, M.1    Debrouwer, D.2
  • 10
    • 0030198540 scopus 로고    scopus 로고
    • Isolation of molecular markers from the barley endosperm coenocyte and the surrounding cell layers
    • Doan, D.N.P., Linnestad, C. and Olsen, O-A. (1996) Isolation of molecular markers from the barley endosperm coenocyte and the surrounding cell layers. Plant Mol. Biol. 31: 877-886.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 877-886
    • Doan, D.N.P.1    Linnestad, C.2    Olsen, O.-A.3
  • 11
    • 0031689628 scopus 로고    scopus 로고
    • Germination-related genes encoding proteolytic enzymes are expressed in the nucellus of developing wheat grains
    • Dominguez, F. and Cejudo, F.J. (1998) Germination-related genes encoding proteolytic enzymes are expressed in the nucellus of developing wheat grains. Plant J. 15: 569-574.
    • (1998) Plant J. , vol.15 , pp. 569-574
    • Dominguez, F.1    Cejudo, F.J.2
  • 12
    • 0034921114 scopus 로고    scopus 로고
    • The nucellus degenerates by a process of programmed cell death during the early stages of wheat grain development
    • Dominguez, F., Moreno, J., and Cejudo, FJ. (2001) The nucellus degenerates by a process of programmed cell death during the early stages of wheat grain development. Planta 213: 352-360.
    • (2001) Planta , vol.213 , pp. 352-360
    • Dominguez, F.1    Moreno, J.2    Cejudo, F.J.3
  • 14
    • 0001244666 scopus 로고    scopus 로고
    • ScanProsite, a reference implementation of a PROSITE scanning tool
    • Gattiker, A., Gasteiger, E. and Bairoch A. (2002) ScanProsite, a reference implementation of a PROSITE scanning tool. Appl. Bioinformatics 1: 107-108.
    • (2002) Appl. Bioinformatics , vol.1 , pp. 107-108
    • Gattiker, A.1    Gasteiger, E.2    Bairoch, A.3
  • 15
    • 0030210553 scopus 로고    scopus 로고
    • Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies
    • Hayashi, M., Aoki, M., Kato, A., Kondo, M. and Nishimura, M. (1996) Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J. 10: 225-234.
    • (1996) Plant J. , vol.10 , pp. 225-234
    • Hayashi, M.1    Aoki, M.2    Kato, A.3    Kondo, M.4    Nishimura, M.5
  • 16
    • 0031154927 scopus 로고    scopus 로고
    • Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide
    • Hayashi, M., Aoki, M., Kondo, M. and Nishimura, M. (1997) Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide. Plant Cell Physiol. 38: 759-768.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 759-768
    • Hayashi, M.1    Aoki, M.2    Kondo, M.3    Nishimura, M.4
  • 17
    • 0037339668 scopus 로고    scopus 로고
    • Nuclease activities and DNA fragmentation during programmed cell death of megagametophyte cells of white spruce (Picea glauca) seeds
    • He, X. and Kermode, A.R. (2003) Nuclease activities and DNA fragmentation during programmed cell death of megagametophyte cells of white spruce (Picea glauca) seeds. Plant Mol. Biol. 51: 509-521.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 509-521
    • He, X.1    Kermode, A.R.2
  • 18
    • 0001282586 scopus 로고
    • In situ hybridization in plants
    • Edited by Bowles, D.J. Gurr, S.J. and Mcphereson, M. Oxford University Press
    • Jackson, D.P. (1991) In situ hybridization in plants. In Molecular Plant Pathology: A Practical Approach. Edited by Bowles, D.J. Gurr, S.J. and Mcphereson, M. pp. 163-174. Oxford University Press,
    • (1991) Molecular Plant Pathology: A Practical Approach , pp. 163-174
    • Jackson, D.P.1
  • 19
    • 0008078622 scopus 로고    scopus 로고
    • Cloning and characterization of an early embryogenesis gene, EEA1 (accession no. AF017430), from barley (PGR97-184)
    • Jung, W., Skadsen, R.W. and Peterson, D.M. (1997) Cloning and characterization of an early embryogenesis gene, EEA1 (accession no. AF017430), from barley (PGR97-184). Plant Physiol. 115: 1730.
    • (1997) Plant Physiol. , vol.115 , pp. 1730
    • Jung, W.1    Skadsen, R.W.2    Peterson, D.M.3
  • 20
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: Inactivation and vacuolar targeting
    • Kervinen, J., Tobin, G.J., Costa, J., Waugh, D.S., Wlodawer, A. and Zdanov, A. (1999) Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J. 18: 3947-3955
    • (1999) EMBO J. , vol.18 , pp. 3947-3955
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 21
    • 0037624063 scopus 로고    scopus 로고
    • Collection, mapping, and annotation of over 28, 000 cDNA clones from japonica rice
    • Kikuchi, S., Satoh, K., Nagata, T., Kawagashira, N., Doi, K., et al. (2003) Collection, mapping, and annotation of over 28, 000 cDNA clones from japonica rice. Science 301: 376-379.
    • (2003) Science , vol.301 , pp. 376-379
    • Kikuchi, S.1    Satoh, K.2    Nagata, T.3    Kawagashira, N.4    Doi, K.5
  • 22
    • 0034191951 scopus 로고    scopus 로고
    • Glycosylation of phytepsin and expression of dad1, dad2 and ost1 during onset of cell death in germinating barley scutella
    • Lindholm, P., Kuittinen, T., Sorri, O., Guo, D., Merits, A., Tormakangas, K. and Runeberg-Roos, P. (2000) Glycosylation of phytepsin and expression of dad1, dad2 and ost1 during onset of cell death in germinating barley scutella. Mech. Dev. 93: 169-173.
    • (2000) Mech. Dev. , vol.93 , pp. 169-173
    • Lindholm, P.1    Kuittinen, T.2    Sorri, O.3    Guo, D.4    Merits, A.5    Tormakangas, K.6    Runeberg-Roos, P.7
  • 23
    • 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.P., 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.P.2    Brown, R.C.3    Lemmon, B.E.4    Meyer, D.J.5    Jung, R.6    Olsen, O.-A.7
  • 24
    • 0032966917 scopus 로고    scopus 로고
    • Cis-elements of protein transport to the plant vacuoles
    • Matsuoka, K. and Neuhaus, J.-M. (1999) Cis-elements of protein transport to the plant vacuoles. J. Exp. Bot. 50: 165-174.
    • (1999) J. Exp. Bot. , vol.50 , pp. 165-174
    • Matsuoka, K.1    Neuhaus, J.-M.2
  • 25
    • 0002612938 scopus 로고    scopus 로고
    • Targeting and import of matrix proteins into peroxisomes
    • Edited by Baker, A. and Graham, I. Kluwer Academic Publishers, Dordrecht
    • Mullen, R.T. (2002) Targeting and import of matrix proteins into peroxisomes. In Plant Peroxisomes, Biochemistry, Cell Biology and Biotechnological Applications. Edited by Baker, A. and Graham, I. pp 339-385. Kluwer Academic Publishers, Dordrecht.
    • (2002) Plant Peroxisomes, Biochemistry, Cell Biology and Biotechnological Applications , pp. 339-385
    • Mullen, R.T.1
  • 26
    • 0345120944 scopus 로고    scopus 로고
    • Plant aspartic proteinases: Enzymes on the way to a function
    • Mutlu, A. and Gal, S. (1999) Plant aspartic proteinases: enzymes on the way to a function. Physiol. Plant. 105: 569-576.
    • (1999) Physiol. Plant. , vol.105 , pp. 569-576
    • Mutlu, A.1    Gal, S.2
  • 27
    • 0032972509 scopus 로고    scopus 로고
    • PSORT, a program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K. and Horton, P. (1999). PSORT, a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24: 34-35.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 28
    • 0031225204 scopus 로고    scopus 로고
    • A novel protein with DNA binding activity from tobacco chloroplast nucleoids
    • Nakano, T., Murakami, S., Shoji, T., Yoshida, S., Yamada, Y. and Sato, F. (1997) A novel protein with DNA binding activity from tobacco chloroplast nucleoids. Plant Cell 9: 1673-1682.
    • (1997) Plant Cell , vol.9 , pp. 1673-1682
    • Nakano, T.1    Murakami, S.2    Shoji, T.3    Yoshida, S.4    Yamada, Y.5    Sato, F.6
  • 29
    • 0029004315 scopus 로고
    • Families of aspartic peptidases and those of unknown catalytic mechanism
    • Rawlings, N.D. and Barrett, A.J. (1995) Families of aspartic peptidases and those of unknown catalytic mechanism. Methods Enzymol. 24: 105-120.
    • (1995) Methods Enzymol. , vol.24 , pp. 105-120
    • Rawlings, N.D.1    Barrett, A.J.2
  • 30
    • 0028425479 scopus 로고
    • The aspartic proteinase of barley is a vacular enzyme that processes probarley leetin in vitro
    • Runeberg-Roos, P., Kervinen, J., Kovaleva, V., Raikhel, N.V. and Gal, S. (1994) The aspartic proteinase of barley is a vacular enzyme that processes probarley leetin 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
  • 31
    • 0032126745 scopus 로고    scopus 로고
    • Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells
    • Runeberg-Roos, P. and Saarma, M. (1998) Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells. Plant J. 15: 139-145.
    • (1998) Plant J. , vol.15 , pp. 139-145
    • Runeberg-Roos, P.1    Saarma, M.2
  • 32
    • 0026321028 scopus 로고
    • Primary structure of a barley-grain aspartic proteinase, a plant aspartic proteinase resembling mammalian cathepsin D
    • Runeberg-Roos, P., Törmäkangas, K. and Östman, A. (1991) Primary structure of a barley-grain aspartic proteinase, a plant aspartic proteinase resembling mammalian cathepsin D. Eur. J. Biochem. 202: 1021-1027.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1021-1027
    • Runeberg-Roos, P.1    Törmäkangas, K.2    Östman, A.3
  • 34
    • 0033613176 scopus 로고    scopus 로고
    • Molecular analysis of NOZZLE, a gene involved in pattern formation and early sporogeneisi during sex organ development in Arabidopsis thaliana
    • Schiefthaler, U., Bansubramanian, S., Sieber, P., Chevakier, D., Wissman, E. and Schneitz, K. (1999) Molecular analysis of NOZZLE, a gene involved in pattern formation and early sporogeneisi during sex organ development in Arabidopsis thaliana. Proc. Natl Acad. Sci. USA 96: 11664-11669.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11664-11669
    • Schiefthaler, U.1    Bansubramanian, S.2    Sieber, P.3    Chevakier, D.4    Wissman, E.5    Schneitz, K.6
  • 35
    • 2942512921 scopus 로고    scopus 로고
    • Structure and function of plant aspartic proteinases
    • Simões, I. and Faro, C. (2004) Structure and function of plant aspartic proteinases. Eur. J. Biochem. 271: 2067-2075.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2067-2075
    • Simões, I.1    Faro, C.2
  • 36
    • 0031743876 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a putative extensin from developing barley grains (Hordenm vulgare L.)
    • Sturaro, M., Linnestad, C., Kleinhofs, A., Olsen, O.-A. and Doan, D.N.P. (1998) Characterization of a cDNA encoding a putative extensin from developing barley grains (Hordenm vulgare L.). J. Exp. Bot. 49: 1935-1944.
    • (1998) J. Exp. Bot. , vol.49 , pp. 1935-1944
    • Sturaro, M.1    Linnestad, C.2    Kleinhofs, A.3    Olsen, O.-A.4    Doan, D.N.P.5
  • 37
    • 0034063594 scopus 로고    scopus 로고
    • 2+-dependent cysteine protease is associated with anoxia-induced root tip death in maize
    • 2+-dependent cysteine protease is associated with anoxia-induced root tip death in maize. J. Exp. Bot. 51: 721-730.
    • (2000) J. Exp. Bot. , vol.51 , pp. 721-730
    • Subbaiah, C.C.1    Kollipara, K.P.2    Sachs, M.M.3
  • 38
    • 0034808250 scopus 로고    scopus 로고
    • A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum
    • Törmäkangas, K., Hadlington, J.L., Pimpl, P., Hillmer, S., Brandizzi, F., Teeri, T.H. and Denecke, J. (2001) A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 13: 2021-2032.
    • (2001) Plant Cell , vol.13 , pp. 2021-2032
    • Törmäkangas, K.1    Hadlington, J.L.2    Pimpl, P.3    Hillmer, S.4    Brandizzi, F.5    Teeri, T.H.6    Denecke, J.7
  • 39
    • 0028317608 scopus 로고
    • Tissue-specific localization of aspartic proteinase in developing and germinating barley grains
    • Törmäkangas, K., Kervinen, J., Östman, A. and Teeri, T. (1994) Tissue-specific localization of aspartic proteinase in developing and germinating barley grains. Planta 195: 116-125.
    • (1994) Planta , vol.195 , pp. 116-125
    • Törmäkangas, K.1    Kervinen, J.2    Östman, A.3    Teeri, T.4
  • 40
    • 0034483033 scopus 로고    scopus 로고
    • Programmed cell death in plant reproduction
    • Wu, H.M. and Cheun, A.Y. (2000) Programmed cell death in plant reproduction. Plant Mol. Biol. 44: 267-281.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 267-281
    • Wu, H.M.1    Cheun, A.Y.2
  • 41
    • 1842614199 scopus 로고    scopus 로고
    • An extracellular aspartic protease functions in Arabidopsis disease resistance signaling
    • Xia, Y., Suzuki, H., Borevitz, J., Blount, J., Guo, Z., Patel, K., Dixon, R.A. and Lamb, C. (2004) An extracellular aspartic protease functions in Arabidopsis disease resistance signaling. EMBO J. 23: 980-988.
    • (2004) EMBO J. , vol.23 , pp. 980-988
    • Xia, Y.1    Suzuki, H.2    Borevitz, J.3    Blount, J.4    Guo, Z.5    Patel, K.6    Dixon, R.A.7    Lamb, C.8
  • 42
    • 0033083491 scopus 로고    scopus 로고
    • Expression of cysteine proteinase during developmental events associated with programmed cell death in brinjal
    • Xu, F.X. and Chye, M.L. (1999) Expression of cysteine proteinase during developmental events associated with programmed cell death in brinjal. Plant J. 17: 321-327.
    • (1999) Plant J. , vol.17 , pp. 321-327
    • Xu, F.X.1    Chye, M.L.2
  • 43
    • 0032510795 scopus 로고    scopus 로고
    • Screening for overlapping bacterial artificial chromosome clones by PCR analysis with an arbitrary primer
    • Xu, J., Yang, D., Domingo, J., Ni, J. and Huang, N. (1998) Screening for overlapping bacterial artificial chromosome clones by PCR analysis with an arbitrary primer. Proc. Natl Acad. Sci. USA 95: 5661-5666.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5661-5666
    • Xu, J.1    Yang, D.2    Domingo, J.3    Ni, J.4    Huang, N.5
  • 44
    • 0033883852 scopus 로고    scopus 로고
    • Cucumber mosaic virus D satellite RNA-induced programmed cell death in tomato
    • Xu, P. and Roossinck, M.J. (2000) Cucumber mosaic virus D satellite RNA-induced programmed cell death in tomato. Plant Cell 12: 1079-1092.
    • (2000) Plant Cell , vol.12 , pp. 1079-1092
    • Xu, P.1    Roossinck, M.J.2


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