메뉴 건너뛰기




Volumn 210, Issue 1, 1998, Pages 45-52

Characterization of a gene from the filamentous fungus Podospora anserina encoding an aspartyl protease induced upon carbon starvation

Author keywords

eapA; papA; Transcriptional regulation; Vegetative incompatibility

Indexed keywords

ASPARTIC PROTEINASE; BOVINE SERUM ALBUMIN; CARBON;

EID: 0032571557     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00057-2     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0025033985 scopus 로고
    • Effects of glycosylation on the secretion and enzyme activity of Mucor renin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast
    • Aikawa J.I., Yamashita T., Nishiyama N., Horinouchi S., Beppu T. Effects of glycosylation on the secretion and enzyme activity of Mucor renin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast. J. Biol. Chem. 265:1990;13955-13959.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13955-13959
    • Aikawa, J.I.1    Yamashita, T.2    Nishiyama, N.3    Horinouchi, S.4    Beppu, T.5
  • 2
    • 0022753540 scopus 로고
    • PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar proteases
    • Ammerer G., Hunter C.P., Rothman J.H., Saari G.C., Valls L.A., Stevens T.H. PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar proteases. Mol. Cell. Biol. 6:1986;2490-2499.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2490-2499
    • Ammerer, G.1    Hunter, C.P.2    Rothman, J.H.3    Saari, G.C.4    Valls, L.A.5    Stevens, T.H.6
  • 3
    • 0022946198 scopus 로고
    • Sequences important for gene expression in filamentous fungi
    • Ballance D.J. Sequences important for gene expression in filamentous fungi. Yeast. 2:1986;229-236.
    • (1986) Yeast , vol.2 , pp. 229-236
    • Ballance, D.J.1
  • 4
    • 0023413790 scopus 로고
    • Amino acid sequence of Endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica
    • Barkholt V. Amino acid sequence of Endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica. Eur. J. Biochem. 167:1987;327-338.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 327-338
    • Barkholt, V.1
  • 5
    • 0010646019 scopus 로고
    • Proteolytic enzymes and protoplasmic incompatibility in Podospora anserina
    • Bégueret J., Bernet J. Proteolytic enzymes and protoplasmic incompatibility in Podospora anserina. Nature New Biol. 243:1973;64-96.
    • (1973) Nature New Biol. , vol.243 , pp. 64-96
    • Bégueret, J.1    Bernet, J.2
  • 6
    • 0027985296 scopus 로고
    • Vegetative incompatibility in filamentous fungus: Het genes begin to talk
    • Bégueret J., Turcq B., Clavé C. Vegetative incompatibility in filamentous fungus: het genes begin to talk. Trends Genet. 10:1994;441-446.
    • (1994) Trends Genet. , vol.10 , pp. 441-446
    • Bégueret, J.1    Turcq, B.2    Clavé, C.3
  • 7
    • 0024546848 scopus 로고
    • Heat-shock at an elevated temperature improves transformation efficiency of protoplasts from Podospora anserina
    • Bergès T., Barreau C. Heat-shock at an elevated temperature improves transformation efficiency of protoplasts from Podospora anserina. J. Gen. Microbiol. 135:1989;601-604.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 601-604
    • Bergès, T.1    Barreau, C.2
  • 8
    • 0025134312 scopus 로고
    • Cloning, sequence and expression of the rat cathepsin D
    • Birch N.P., Peng Loh Y. Cloning, sequence and expression of the rat cathepsin D. Nucleic Acids Res. 18:1990;6445-6446.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6445-6446
    • Birch, N.P.1    Peng Loh, Y.2
  • 9
    • 0019888969 scopus 로고
    • Polypeptide synthesis during protoplasmic incompatibility in the fungus Podospora anserina
    • Boucherie H., Dupont C.H., Bernet J. Polypeptide synthesis during protoplasmic incompatibility in the fungus Podospora anserina. Biochem. Biophys. Acta. 653:1981;18-26.
    • (1981) Biochem. Biophys. Acta , vol.653 , pp. 18-26
    • Boucherie, H.1    Dupont, C.H.2    Bernet, J.3
  • 10
    • 0027522469 scopus 로고
    • Molecular cloning and overexpression of the gene encoding endothiapepsin, an aspartic protease from Chryphonectria parasitica
    • Choi G.H., Pawlyk D.M., Rae B., Shapira R., Nuss D.L. Molecular cloning and overexpression of the gene encoding endothiapepsin, an aspartic protease from Chryphonectria parasitica. Gene. 125:1993;135-141.
    • (1993) Gene , vol.125 , pp. 135-141
    • Choi, G.H.1    Pawlyk, D.M.2    Rae, B.3    Shapira, R.4    Nuss, D.L.5
  • 11
    • 0017379372 scopus 로고
    • Regulation of exocellular protease in Neurospora crassa: Induction and repression under conditions of nitrogen starvation
    • Cohen B.L., Drucker H. Regulation of exocellular protease in Neurospora crassa: induction and repression under conditions of nitrogen starvation. Arch. Biochem. Biophys. 182:1977;601-613.
    • (1977) Arch. Biochem. Biophys. , vol.182 , pp. 601-613
    • Cohen, B.L.1    Drucker, H.2
  • 12
    • 0027234098 scopus 로고
    • A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina
    • Deleu C., Clavé C., Bégueret J. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics. 135:1993;45-52.
    • (1993) Genetics , vol.135 , pp. 45-52
    • Deleu, C.1    Clavé, C.2    Bégueret, J.3
  • 13
    • 0000912663 scopus 로고
    • Podospora aserina
    • In: King, R.C. (Ed.), Plenum Press, New York
    • Esser, K., 1974. Podospora aserina. In: King, R.C. (Ed.), Handbook of Genetics. Plenum Press, New York, pp. 531-551.
    • (1974) Handbook of Genetics , pp. 531-551
    • Esser, K.1
  • 14
    • 0020685129 scopus 로고
    • Structure and refinement of penicillopepsin at 1,8 Å resolution
    • James M.N., Sielecki A.R. Structure and refinement of penicillopepsin at 1,8 Å resolution. J. Mol. Biol. 163:1983;299-361.
    • (1983) J. Mol. Biol. , vol.163 , pp. 299-361
    • James, M.N.1    Sielecki, A.R.2
  • 15
    • 0028093358 scopus 로고
    • Nitrogen, carbon and pH dependence of extracellular acidic proteases of Aspergillus niger
    • Jarai G., Buxton F. Nitrogen, carbon and pH dependence of extracellular acidic proteases of Aspergillus niger. Curr. Genet. 26:1994;238-244.
    • (1994) Curr. Genet. , vol.26 , pp. 238-244
    • Jarai, G.1    Buxton, F.2
  • 16
    • 0026640551 scopus 로고
    • Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky D.J., Cueva R., Yaver D.S. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J. Cell. Biol. 119:1992;287-299.
    • (1992) J. Cell. Biol. , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 17
    • 17044448865 scopus 로고
    • Propriétés d'un système d'incompatibilité chez le champignon filamenteux P. anserina et intérêt de ce système pour l'étude de l'incompatibilité
    • Labarère J. Propriétés d'un système d'incompatibilité chez le champignon filamenteux P. anserina et intérêt de ce système pour l'étude de l'incompatibilité C.R. Acad. Sci. Paris. 276:1973;1301-1304.
    • (1973) C.R. Acad. Sci. Paris , vol.276 , pp. 1301-1304
    • Labarère, J.1
  • 18
    • 0028069681 scopus 로고
    • Rapid methods for nucleic acids extraction from petri-dish grown mycelia
    • Lecellier G., Silar P. Rapid methods for nucleic acids extraction from petri-dish grown mycelia. Curr. Genet. 25:1994;122-123.
    • (1994) Curr. Genet. , vol.25 , pp. 122-123
    • Lecellier, G.1    Silar, P.2
  • 19
    • 0343408149 scopus 로고    scopus 로고
    • An additional copy of the adenylate cyclase encoding gene relieves developmental defects produced by a mutation in a vegetative incompatibility controlling gene in Podospora anserina
    • Loubradou G., Bégueret J., Turcq B. An additional copy of the adenylate cyclase encoding gene relieves developmental defects produced by a mutation in a vegetative incompatibility controlling gene in Podospora anserina. Gene. 170:1996;119-123.
    • (1996) Gene , vol.170 , pp. 119-123
    • Loubradou, G.1    Bégueret, J.2    Turcq, B.3
  • 20
    • 0030794656 scopus 로고    scopus 로고
    • Genetic regulation of nitrogen metabolism in the fungi
    • Marzluf G.A. Genetic regulation of nitrogen metabolism in the fungi. Mol. Biol. Rev. 61:1997;17-32.
    • (1997) Mol. Biol. Rev. , vol.61 , pp. 17-32
    • Marzluf, G.A.1
  • 21
    • 0028173191 scopus 로고
    • A cosmid with a HyR marker for fungal library construction and screening
    • Orbach M.J. A cosmid with a HyR marker for fungal library construction and screening. Gene. 150:1994;159-162.
    • (1994) Gene , vol.150 , pp. 159-162
    • Orbach, M.J.1
  • 22
    • 0023512725 scopus 로고
    • Transformation of Aspergillus nidulans based on the hygromycin B resistance marker from Escherichia coli
    • Punt P.J., Oliver R.P., Dingemause M.A., Pouwels P.H., van Den Hondel C.A.M.J.J. Transformation of Aspergillus nidulans based on the hygromycin B resistance marker from Escherichia coli. Gene. 56:1987;117-124.
    • (1987) Gene , vol.56 , pp. 117-124
    • Punt, P.J.1    Oliver, R.P.2    Dingemause, M.A.3    Pouwels, P.H.4    Van Den Hondel, C.A.M.J.J.5
  • 24
    • 0023815375 scopus 로고
    • Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell
    • Rendueles P.S., Wolf D.H. Proteinase function in yeast: biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell. FEMS Microbiol. Rev. 54:1988;17-46.
    • (1988) FEMS Microbiol. Rev. , vol.54 , pp. 17-46
    • Rendueles, P.S.1    Wolf, D.H.2
  • 25
    • 0028835605 scopus 로고
    • Glucose repression in fungi
    • Ronne H. Glucose repression in fungi. Trends Genet. 11:1995;12-17.
    • (1995) Trends Genet. , vol.11 , pp. 12-17
    • Ronne, H.1
  • 27
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • Tang J., Wong R.N.S. Evolution in the structure and function of aspartic proteases. J. Cell. Biochem. 33:1987;53-63.
    • (1987) J. Cell. Biochem. , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.S.2
  • 28
    • 0023260610 scopus 로고
    • The ura 5 gene of the filamentous fungus Podospora anserina: Nucleotide sequence and expression in transformed strains
    • Turcq B., Bégueret J. The ura 5 gene of the filamentous fungus Podospora anserina: nucleotide sequence and expression in transformed strains. Gene. 53:1987;201-209.
    • (1987) Gene , vol.53 , pp. 201-209
    • Turcq, B.1    Bégueret, J.2
  • 29
    • 0029064193 scopus 로고
    • Secretion and maturation of endothiapepsin in Saccharomyces cerevisiae
    • Valverde V., Delmas P., Kaghad M., Loison G., Jara P. Secretion and maturation of endothiapepsin in Saccharomyces cerevisiae. J. Biol. Chem. 270:1995;15821-15826.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15821-15826
    • Valverde, V.1    Delmas, P.2    Kaghad, M.3    Loison, G.4    Jara, P.5
  • 30
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:1986;4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.