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Volumn 29, Issue 5, 1996, Pages 474-481

Expression of an Erwinia pectate lyase in three species of Aspergillus

Author keywords

Expression; Glycosylation; Processing; Proteolytic degradation

Indexed keywords

ASPERGILLUS; ASPERGILLUS AWAMORI; ASPERGILLUS NIGER; ERWINIA; FUNGI; PECTOBACTERIUM ATROSEPTICUM; PECTOBACTERIUM CAROTOVORUM;

EID: 0030117868     PISSN: 01728083     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf02221517     Document Type: Article
Times cited : (12)

References (45)
  • 1
    • 0029059886 scopus 로고
    • Synergism between Erwima pectate lyase isoenzymes that de-polymerize both pectate and pectin
    • Bartling S, Wegener C, Olsen O (1995) Synergism between Erwima pectate lyase isoenzymes that de-polymerize both pectate and pectin. Microbiology 141:873-881
    • (1995) Microbiology , vol.141 , pp. 873-881
    • Bartling, S.1    Wegener, C.2    Olsen, O.3
  • 3
    • 0025018051 scopus 로고
    • Molecular cloning, nucleotide sequence and expression of the gene encoding prepropolygalacturonase II of Aspergillus niger
    • Bussink HJD, Kester HCM, Visser J (1990) Molecular cloning, nucleotide sequence and expression of the gene encoding prepropolygalacturonase II of Aspergillus niger. FEBS Lett 1,2:127-130
    • (1990) FEBS Lett , vol.1-2 , pp. 127-130
    • Bussink, H.J.D.1    Kester, H.C.M.2    Visser, J.3
  • 4
    • 0025778260 scopus 로고
    • Expression and sequence comparison of the Aspergillus niger and Aspergillus tubigensis genes encoding polygalacturonase II
    • Bussink HJD, Buxton FP, Visser J (1991) Expression and sequence comparison of the Aspergillus niger and Aspergillus tubigensis genes encoding polygalacturonase II. Curr Genet 19:467-474
    • (1991) Curr Genet , vol.19 , pp. 467-474
    • Bussink, H.J.D.1    Buxton, F.P.2    Visser, J.3
  • 5
    • 0015892141 scopus 로고
    • The neutral and alkaline proteases of Aspergillus nidulans
    • Cohen BL (1973) The neutral and alkaline proteases of Aspergillus nidulans. J Gen Microbiol 77:521-528
    • (1973) J Gen Microbiol , vol.77 , pp. 521-528
    • Cohen, B.L.1
  • 6
    • 0000980748 scopus 로고
    • The role of pectic enzymes in plant pathogenesis
    • Collmer A, Keen NT (1986) The role of pectic enzymes in plant pathogenesis Annu Rev Phytopathol 24:383-409
    • (1986) Annu Rev Phytopathol , vol.24 , pp. 383-409
    • Collmer, A.1    Keen, N.T.2
  • 7
    • 14744271483 scopus 로고
    • Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergillus niger and secretion of mature interleukin-6
    • Contreras R, Carrez D, Kinghorn JR, van den Hondel CAMJJ, Fiers W (1991) Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergillus niger and secretion of mature interleukin-6. Bio/Technol 9:378-381
    • (1991) Bio/Technol , vol.9 , pp. 378-381
    • Contreras, R.1    Carrez, D.2    Kinghorn, J.R.3    Van Den Hondel, C.A.M.J.J.4    Fiers, W.5
  • 8
    • 0017855795 scopus 로고
    • Estimation of the Michaelis constant and maximum velocity from the direct linear plot
    • Cornish-Bowden A, Eisenthal R (1978) Estimation of the Michaelis constant and maximum velocity from the direct linear plot. Biochim Biophys Acta 523:268-272
    • (1978) Biochim Biophys Acta , vol.523 , pp. 268-272
    • Cornish-Bowden, A.1    Eisenthal, R.2
  • 9
    • 0028186186 scopus 로고
    • Heterologous gene expression and protein secretion in Aspergillus
    • Davies RW (1994) Heterologous gene expression and protein secretion in Aspergillus. Prog Ind Microbiol 29:527-560
    • (1994) Prog Ind Microbiol , vol.29 , pp. 527-560
    • Davies, R.W.1
  • 10
    • 0024619547 scopus 로고
    • Regulation of the Aspergillus nidulans pectate lyase gene (pelA)
    • Dean RA, Timberlake WE (1989) Regulation of the Aspergillus nidulans pectate lyase gene (pelA). Plant Cell 1:275-284
    • (1989) Plant Cell , vol.1 , pp. 275-284
    • Dean, R.A.1    Timberlake, W.E.2
  • 11
    • 0026098320 scopus 로고
    • Expression of heterologous proteins in Aspergillus
    • Devchand M, Gwynne DI (1991) Expression of heterologous proteins in Aspergillus. J Biotechnol 17:3-10
    • (1991) J Biotechnol , vol.17 , pp. 3-10
    • Devchand, M.1    Gwynne, D.I.2
  • 13
  • 14
    • 0023947436 scopus 로고
    • Isolation and transformation of the pyruvate kinase gene of Aspergillus nidulans
    • Graaff LH de, van den Broeck HC, Visser J (1988) Isolation and transformation of the pyruvate kinase gene of Aspergillus nidulans. Curr Genet 13:315-321
    • (1988) Curr Genet , vol.13 , pp. 315-321
    • De Graaff, L.H.1    Van Den Broeck, H.C.2    Visser, J.3
  • 15
    • 0026691942 scopus 로고
    • Isolation and characterization of the Aspergillus niger pyruvate kinase gene
    • Graaff de LH, van den Broeck HC, Visser J (1992) Isolation and characterization of the Aspergillus niger pyruvate kinase gene. Curr Genet 22:21-27
    • (1992) Curr Genet , vol.22 , pp. 21-27
    • De Graaff, L.H.1    Van Den Broeck, H.C.2    Visser, J.3
  • 17
    • 0021770334 scopus 로고
    • How signal sequences maintain cleavage specificity
    • Heijne G von (1984) How signal sequences maintain cleavage specificity. J Mol Biol 173:243-251
    • (1984) J Mol Biol , vol.173 , pp. 243-251
    • Von Heijne, G.1
  • 18
    • 0028898476 scopus 로고
    • Sequence analysis of the Aspergillus nidulans pectate lyase pelA gene and evidence for binding of promotor regions to CREA, a regulator of carbon catabolite repression
    • Ho M-C, Whitehead MP, Cleveland TE, Dean RA (1995) Sequence analysis of the Aspergillus nidulans pectate lyase pelA gene and evidence for binding of promotor regions to CREA, a regulator of carbon catabolite repression. Curr Genet 27:142-149
    • (1995) Curr Genet , vol.27 , pp. 142-149
    • Ho, M.-C.1    Whitehead, M.P.2    Cleveland, T.E.3    Dean, R.A.4
  • 19
    • 0028574789 scopus 로고
    • Cloninig, characterization and expression of pepF, a serine carboxypeptidase from Aspergillus niger
    • van den Hombergh JPTW, Jarai G, Buxton FP, Visser J (1994) Cloninig, characterization and expression of pepF, a serine carboxypeptidase from Aspergillus niger. Gene 151:73-79
    • (1994) Gene , vol.151 , pp. 73-79
    • Van Den Hombergh, J.P.T.W.1    Jarai, G.2    Buxton, F.P.3    Visser, J.4
  • 20
    • 0029100574 scopus 로고
    • New protease mutants in Aspergillus niger result in strongly reduced in vitro degradation of target proteins, genetic and biochemical characterization of seven complementation groups
    • van den Hombergh JPTW, van de Vondervoort PJI, van der Heijden NCBA, Visser J (1995) New protease mutants in Aspergillus niger result in strongly reduced in vitro degradation of target proteins, genetic and biochemical characterization of seven complementation groups. Curr Genet 28:299-308
    • (1995) Curr Genet , vol.28 , pp. 299-308
    • Van Den Hombergh, J.P.T.W.1    Van De Vondervoort, P.J.I.2    Van Der Heijden, N.C.B.A.3    Visser, J.4
  • 22
    • 0028093358 scopus 로고
    • Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger
    • Jarai G, Buxton FP (1994) Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger. Curr Genet 26:238-244
    • (1994) Curr Genet , vol.26 , pp. 238-244
    • Jarai, G.1    Buxton, F.P.2
  • 23
    • 0028568211 scopus 로고
    • Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease
    • Katz ME, Rice RN, Cheetham BF (1994) Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease. Gene 150:287-292
    • (1994) Gene , vol.150 , pp. 287-292
    • Katz, M.E.1    Rice, R.N.2    Cheetham, B.F.3
  • 24
    • 0025910182 scopus 로고
    • The structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans
    • Kusters-van Someren MA, Harmsen JAM, Kester HCM, Visser J (1991) The structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans. Curr Genet 20:293-299
    • (1991) Curr Genet , vol.20 , pp. 293-299
    • Kusters-van Someren, M.A.1    Harmsen, J.A.M.2    Kester, H.C.M.3    Visser, J.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 26
    • 0026062588 scopus 로고
    • Isolation and nucleotide sequence of the Aspergillus restricteus gene encoding for the ribonucleolytic toxin restrictocin and its expression in Aspergillus niger: The leader sequence protects producing strains from suicide
    • Lamy B, Davies J (1991) Isolation and nucleotide sequence of the Aspergillus restricteus gene encoding for the ribonucleolytic toxin restrictocin and its expression in Aspergillus niger: the leader sequence protects producing strains from suicide. Nucleic Acids Res 19:1001-1006
    • (1991) Nucleic Acids Res , vol.19 , pp. 1001-1006
    • Lamy, B.1    Davies, J.2
  • 27
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley F, Trimble RB, Tarentino AL, Plummer Jr TH (1989) Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem 180:195-204
    • (1989) Anal Biochem , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 30
    • 0014028077 scopus 로고
    • Polygalacturonase of Erwinia carotovora
    • Nasuno S, Starr MP (1966) Polygalacturonase of Erwinia carotovora. J Biol Chem 241:5298-5306
    • (1966) J Biol Chem , vol.241 , pp. 5298-5306
    • Nasuno, S.1    Starr, M.P.2
  • 32
    • 0026468312 scopus 로고
    • A rapid method for preparing multiple DNA fusions
    • Olsen O (1992) A rapid method for preparing multiple DNA fusions. Meth Mol Cell Biol 3:159-160
    • (1992) Meth Mol Cell Biol , vol.3 , pp. 159-160
    • Olsen, O.1
  • 34
    • 0025806975 scopus 로고
    • Molecular biology of Erwinia: From soft-rot to antileucaemics
    • Robert-Baudouy J (1991) Molecular biology of Erwinia: from soft-rot to antileucaemics. Trends Biotechnol 9:325-329
    • (1991) Trends Biotechnol , vol.9 , pp. 325-329
    • Robert-Baudouy, J.1
  • 37
    • 0025576522 scopus 로고
    • Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize
    • Scott-Craig JS, Panaccione DG, Cervone F, Walton JD (1990) Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 2:1191-1200
    • (1990) Plant Cell , vol.2 , pp. 1191-1200
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Cervone, F.3    Walton, J.D.4
  • 38
    • 0025211918 scopus 로고
    • Ustilago maydis KP6 killer toxin: Structure, expression in Saccharomyces cerevisiae, and relationships to other cellular toxins
    • Tao J, Ginsberg I, Banerjee N, Held W, Koltin Y, Bruenn JA (1990) Ustilago maydis KP6 killer toxin: structure, expression in Saccharomyces cerevisiae, and relationships to other cellular toxins. Mol Cell Biol 10:1373-1381
    • (1990) Mol Cell Biol , vol.10 , pp. 1373-1381
    • Tao, J.1    Ginsberg, I.2    Banerjee, N.3    Held, W.4    Koltin, Y.5    Bruenn, J.A.6
  • 39
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulytic enzymes: Gene sequence and expression of cellobiohydrolase II
    • Teeri TT, Lehtovaara P, Kauppinen S, Salovuori I, Knowles J (1987) Homologous domains in Trichoderma reesei cellulytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51:43-52
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovuori, I.4    Knowles, J.5
  • 40
    • 0029077782 scopus 로고
    • Molecular genetic strain improvement for the overproduction of fungal proteins by filamentous fungi
    • Verdoes JC, Punt PJ, van den Hondel CAMJJ (1995) Molecular genetic strain improvement for the overproduction of fungal proteins by filamentous fungi. Appl Microbiol Biotechnol 43:195-205
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 195-205
    • Verdoes, J.C.1    Punt, P.J.2    Van Den Hondel, C.A.M.J.J.3
  • 42
    • 0000253313 scopus 로고
    • Gene expression in filamentous fungi; expression of pectinases and glucose oxidase in Aspergillus niger
    • Smith A (ed) Marcel Dekker Inc. New York
    • Visser J, Bussink H-J, Witteveen C (1994) Gene expression in filamentous fungi; expression of pectinases and glucose oxidase in Aspergillus niger. In: Smith A (ed) Gene expression in recombinant microorganisms. Marcel Dekker Inc. New York, pp 241-308
    • (1994) Gene Expression in Recombinant Microorganisms , pp. 241-308
    • Visser, J.1    Bussink, H.-J.2    Witteveen, C.3
  • 45
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder MD, Keen NT, Jurnak F (1993) New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260:1503-1506
    • (1993) Science , vol.260 , pp. 1503-1506
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.