메뉴 건너뛰기




Volumn 152, Issue 6, 1998, Pages 675-682

A vacuolar cysteine endopeptidase (SH-EP) that digests seed storage globulin: Characterization, regulation of gene expression, and posttranslational processing

Author keywords

Cysteine endopeptidase EC 3.4.22. ; Posttranslational processing; Seed storage protein; Vacuolar proteinase; Vigna mungo

Indexed keywords

VIGNA MUNGO;

EID: 0031818789     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0176-1617(98)80029-1     Document Type: Conference Paper
Times cited : (31)

References (38)
  • 2
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH- EP) from cotyledons of germinating Vigna mungo seeds
    • H. Akasofu D. Yamauchi W. Mitsuhashi T. Minamikawa Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH- EP) from cotyledons of germinating Vigna mungo seeds Nucleic Acids Res. 17 1989 6733
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6733
    • Akasofu, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 3
    • 0025317953 scopus 로고
    • Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP)
    • H. Akasofu D. Yamauchi T. Minamikawa Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP) Nucleic Acids Res. 18 1990 1892
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1892
    • Akasofu, H.1    Yamauchi, D.2    Minamikawa, T.3
  • 4
    • 0017407885 scopus 로고
    • Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings
    • B. Baumgartner M.J. Chrispeels Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings Eur. J. Biochem. 77 1977 223 233
    • (1977) Eur. J. Biochem. , vol.77 , pp. 223-233
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 5
    • 0003029728 scopus 로고
    • The development of proteolytic activity and protein degradation during the germination of Pisum sativum L
    • S.M.M. Basha L. Beevers The development of proteolytic activity and protein degradation during the germination of Pisum sativum L Planta 124 1975 77 87
    • (1975) Planta , vol.124 , pp. 77-87
    • Basha, S.M.M.1    Beevers, L.2
  • 6
    • 0028535314 scopus 로고
    • PCR cloning and expression analysis of cONAs encoding cysteine proteinases from germinating seeds of Vicia sativa L
    • C. Becker J. Fischer V.H. Nong K. Müntz PCR cloning and expression analysis of cONAs encoding cysteine proteinases from germinating seeds of Vicia sativa L Plant Mol. Biol. 26 1994 1207 1212
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1207-1212
    • Becker, C.1    Fischer, J.2    Nong, V.H.3    Müntz, K.4
  • 7
    • 0028958785 scopus 로고
    • Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch ( Vicia sativa L.) seeds
    • C. Becker A.D. Shutov V.H. Nong V.I. Senyuk R. Jung C. Horstmann J. Fischer N.C. Nielsen K. Müntz Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch ( Vicia sativa L.) seeds Eur. J. Biochem. 228 1995 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    Müntz, K.9
  • 8
    • 85119813041 scopus 로고
    • J.D. Bewley M. Black Seeds Physiology of Development and Germination 2nd ed. 1994 Plenum Press New York and London 232 338
    • (1994) , pp. 232-338
    • Bewley, J.D.1    Black Seeds, M.2
  • 9
    • 0000434454 scopus 로고
    • Purification of an endopeptidase involved with storage-protein degradation in Phaseolus vulgaris L
    • M.T. Boylan I.M. Sussex Purification of an endopeptidase involved with storage-protein degradation in Phaseolus vulgaris L cotyledons. Planta 170 1987 343 352
    • (1987) cotyledons. Planta , vol.170 , pp. 343-352
    • Boylan, M.T.1    Sussex, I.M.2
  • 10
    • 0026953035 scopus 로고
    • A gibberellin-regulated gene from wheat with sequence homology to cathepsin B of mammalian cells
    • F.J. Cejudo G. Murphy C. Chinoy D.C. Baulcombe A gibberellin-regulated gene from wheat with sequence homology to cathepsin B of mammalian cells Plant J. 2 1992 937 948
    • (1992) Plant J. , vol.2 , pp. 937-948
    • Cejudo, F.J.1    Murphy, G.2    Chinoy, C.3    Baulcombe, D.C.4
  • 12
    • 0001743127 scopus 로고
    • Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase
    • M.J. Chrispeels D. Boulter Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase Plant Physiol. 55 1975 1031 1037
    • (1975) Plant Physiol. , vol.55 , pp. 1031-1037
    • Chrispeels, M.J.1    Boulter, D.2
  • 13
    • 0027688051 scopus 로고
    • Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • I. Hara-Nishimura Y. Takeuchi M. Nishimura Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni Plant Cell 5 1993 1651 1659
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 14
    • 0028721072 scopus 로고
    • Gibberellins: perception, transduction and responses
    • R. Hooley Gibberellins: perception, transduction and responses Plant Mol. Biol. 26 1994 1529 1555
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1529-1555
    • Hooley, R.1
  • 15
    • 0028673279 scopus 로고
    • Legumain: asparaginyl endopeptidase
    • S. Ishi Legumain: asparaginyl endopeptidase Methods Enzymol. 244 1994 604 615
    • (1994) Methods Enzymol. , vol.244 , pp. 604-615
    • Ishi, S.1
  • 16
    • 0001516815 scopus 로고
    • Studies of sites of action of a new plant growth retardant (E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazol-1-yl)-1-penten-3-ol (S-3307) and comparative effects of its stereoisomers in a cell-free system from Cucurbita maxima
    • K. Izumi Y. Kamiya A. Sakurai H. Oshio N. Takahashi Studies of sites of action of a new plant growth retardant (E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazol-1-yl)-1-penten-3-ol (S-3307) and comparative effects of its stereoisomers in a cell-free system from Cucurbita maxima Plant Cell Physiol. 26 1985 821 827
    • (1985) Plant Cell Physiol. , vol.26 , pp. 821-827
    • Izumi, K.1    Kamiya, Y.2    Sakurai, A.3    Oshio, H.4    Takahashi, N.5
  • 17
    • 0029199209 scopus 로고
    • Current status and future strategies of in vitro culture techniques for genetic improvement of mungbean (Vigna radiata (L.) Wilczek)
    • P.K. Jaiwal A. Gulati Current status and future strategies of in vitro culture techniques for genetic improvement of mungbean ( Vigna radiata (L.) Wilczek) Euphytica 86 1995 167 181
    • (1995) Euphytica , vol.86 , pp. 167-181
    • Jaiwal, P.K.1    Gulati, A.2
  • 18
    • 0022643093 scopus 로고
    • Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution
    • M.N.G. James A.R. Sielecki Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution Nature 319 1986 33 38
    • (1986) Nature , vol.319 , pp. 33-38
    • James, M.N.G.1    Sielecki, A.R.2
  • 19
    • 0022429212 scopus 로고
    • Thiol proteases: comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
    • I.G. Kamphuis J. Drenth E.N. Baker Thiol proteases: comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain J. Mol. Biol. 182 1985 317 329
    • (1985) J. Mol. Biol. , vol.182 , pp. 317-329
    • Kamphuis, I.G.1    Drenth, J.2    Baker, E.N.3
  • 20
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • K.M. Karrer S.L. Peiffr M.E. Di Tomas Two distinct gene subfamilies within the family of cysteine protease genes Proc. Nad. Acad. Sci. USA. 90 1993 3063 3067
    • (1993) Proc. Nad. Acad. Sci. USA. , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffr, S.L.2    Di Tomas, M.E.3
  • 21
    • 0025465440 scopus 로고
    • Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers
    • S.M. Koehler T.-H.D. Ho Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers Plant Cell 2 1990 769 783
    • (1990) Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 22
    • 51249182231 scopus 로고
    • Hydrolytic enzyme activities and degradation of storage components in cotyledons of germinating Phaseolus mungo seeds
    • T. Minamikawa Hydrolytic enzyme activities and degradation of storage components in cotyledons of germinating Phaseolus mungo seeds Bot. Mag. Tokyo 92 1979 1 12
    • (1979) Bot. Mag. Tokyo , vol.92 , pp. 1-12
    • Minamikawa, T.1
  • 23
    • 0030152393 scopus 로고    scopus 로고
    • A major cysteine proteinase, EPB, in germinating barley seeds: structure of two intronless genes and regulation of expression
    • A. Mikkonen I. Porali M. Cercos T.D. Ho A major cysteine proteinase, EPB, in germinating barley seeds: structure of two intronless genes and regulation of expression Plant Mol. Biol. 31 1996 239 254
    • (1996) Plant Mol. Biol. , vol.31 , pp. 239-254
    • Mikkonen, A.1    Porali, I.2    Cercos, M.3    Ho, T.D.4
  • 24
    • 0001076074 scopus 로고
    • Separation and characterization of two endopeptidases from cotyledons of germinating Vigna mungo seeds
    • W. Mitsuhashi T. Koshiba T. Minamikawa Separation and characterization of two endopeptidases from cotyledons of germinating Vigna mungo seeds Plant Physiol. 80 1986 628 634
    • (1986) Plant Physiol. , vol.80 , pp. 628-634
    • Mitsuhashi, W.1    Koshiba, T.2    Minamikawa, T.3
  • 25
    • 84897583639 scopus 로고
    • Synthesis and posttransla-tional activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds
    • W. Mitsuhashi T. Minamikawa Synthesis and posttransla-tional activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds Plant Physiol. 89 1989 274 279
    • (1989) Plant Physiol. , vol.89 , pp. 274-279
    • Mitsuhashi, W.1    Minamikawa, T.2
  • 26
    • 0001064980 scopus 로고    scopus 로고
    • Proteinases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • K. Müntz Proteinases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds J. Exp. Bot. 47 1996 605 622
    • (1996) J. Exp. Bot. , vol.47 , pp. 605-622
    • Müntz, K.1
  • 27
    • 0001129084 scopus 로고
    • Degradation of the major storage protein of Phaseolus vulgaris during germination — role of endogenous proteases and protease inhibitors
    • S.S. Nielsen I.E. Liener Degradation of the major storage protein of Phaseolus vulgaris during germination — role of endogenous proteases and protease inhibitors Plant Physiol. 74 1984 494 498
    • (1984) Plant Physiol. , vol.74 , pp. 494-498
    • Nielsen, S.S.1    Liener, I.E.2
  • 28
    • 0029008688 scopus 로고
    • Purification of a processing enzyme (VmPE-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP)
    • T. Okamoto T. Minamikawa Purification of a processing enzyme (VmPE-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP) Eur. J. Biochem. 231 1995 300 305
    • (1995) Eur. J. Biochem. , vol.231 , pp. 300-305
    • Okamoto, T.1    Minamikawa, T.2
  • 29
    • 0030025445 scopus 로고    scopus 로고
    • Asparaginyl endopeptidase in developing and germinating legume seeds: immunological detection and quantitation
    • T. Okamoto Y. Miura-Izu S. Ishi T. Minamikawa Asparaginyl endopeptidase in developing and germinating legume seeds: immunological detection and quantitation Plant Sei. 115 1996 49 57
    • (1996) Plant Sei. , vol.115 , pp. 49-57
    • Okamoto, T.1    Miura-Izu, Y.2    Ishi, S.3    Minamikawa, T.4
  • 30
    • 0028041312 scopus 로고
    • Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)
    • T. Okamoto H. Nakayama K. Seta T. Isobe T. Minamikawa Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP) FEBS Lett. 351 1994 31 34
    • (1994) FEBS Lett. , vol.351 , pp. 31-34
    • Okamoto, T.1    Nakayama, H.2    Seta, K.3    Isobe, T.4    Minamikawa, T.5
  • 31
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • H.R.B. Pelham Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment EMBO J. 7 1988 913 918
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.B.1
  • 32
    • 0028446555 scopus 로고
    • Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms
    • T. Shimada N. Hiratwa M. Nishimura I. Hara-Nishimura Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms Plant Cell Physiol. 35 1994 713 718
    • (1994) Plant Cell Physiol. , vol.35 , pp. 713-718
    • Shimada, T.1    Hiratwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 33
    • 0000024298 scopus 로고
    • Degradation of storage proteins in germinating seeds
    • A.D. Shutov I.A. Vaintraub Degradation of storage proteins in germinating seeds Phytochemistry 26 1987 1557 1566
    • (1987) Phytochemistry , vol.26 , pp. 1557-1566
    • Shutov, A.D.1    Vaintraub, I.A.2
  • 34
    • 0030041455 scopus 로고    scopus 로고
    • Development of endopeptidase activity in cotyledons of Vigna mungo seedlings: Effects of exogenously applied end-products and plant hormones
    • M. Taneyama T. Okamoto D. Yamauchi T. Minamikawa Development of endopeptidase activity in cotyledons of Vigna mungo seedlings: Effects of exogenously applied end-products and plant hormones Plant Cell Physiol. 37 1996 19 26
    • (1996) Plant Cell Physiol. , vol.37 , pp. 19-26
    • Taneyama, M.1    Okamoto, T.2    Yamauchi, D.3    Minamikawa, T.4
  • 35
    • 0025282543 scopus 로고
    • Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal
    • D. Vaux J. Tooze S. Fuller Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal Nature 345 1990 495 502
    • (1990) Nature , vol.345 , pp. 495-502
    • Vaux, D.1    Tooze, J.2    Fuller, S.3
  • 36
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • P. Walter G. Blobel Preparation of microsomal membranes for cotranslational protein translocation Methods Enzymol. 96 1983 84 93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 37
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains)
    • H. Watanabe K. Abe Y. Emori H. Hosoyama S. Arai Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains) J. Biol. Chem. 266 1991 16897 16902
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.5
  • 38
    • 0000220251 scopus 로고
    • Cysteine endopeptidase from Vigna mungo: gene structure arid expression
    • D. Yamauchi H. Akasofu T. Minamikawa Cysteine endopeptidase from Vigna mungo : gene structure arid expression Plant Cell Physiol. 33 1992 789 797
    • (1992) Plant Cell Physiol. , vol.33 , pp. 789-797
    • Yamauchi, D.1    Akasofu, H.2    Minamikawa, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.