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Volumn 155, Issue 11, 2009, Pages 3673-3682

Characterization of a multimeric, eukaryotic prolyl aminopeptidase: An inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii

Author keywords

[No Author keywords available]

Indexed keywords

AGAR; AMMONIUM SULFATE; GLUCOSE; HYDROLASE; MESSENGER RNA; PROLINE IMINOPEPTIDASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR TEPAP; UNCLASSIFIED DRUG;

EID: 70450230325     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.030940-0     Document Type: Article
Times cited : (30)

References (44)
  • 1
    • 0007919787 scopus 로고
    • Guayule rubber: Microbiological improvement by shrub retting
    • Allen, P. J. & Emerson, R. (1949). Guayule rubber: microbiological improvement by shrub retting. Ind Eng Chem 41, 346-365.
    • (1949) Ind Eng Chem , vol.41 , pp. 346-365
    • Allen, P.J.1    Emerson, R.2
  • 2
    • 0034858599 scopus 로고    scopus 로고
    • Lysine aminopeptidase of Aspergillus niger
    • Basten, D. E., Visser, J. & Schaap, P. J. (2001). Lysine aminopeptidase of Aspergillus niger. Microbiology 147, 2045-2050.
    • (2001) Microbiology , vol.147 , pp. 2045-2050
    • Basten, D.E.1    Visser, J.2    Schaap, P.J.3
  • 3
    • 0346667191 scopus 로고    scopus 로고
    • Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase
    • Basten, D. E., Dekker, P. J. & Schaap, P. J. (2003). Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase. Appl Environ Microbiol 69, 1246-1250.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1246-1250
    • Basten, D.E.1    Dekker, P.J.2    Schaap, P.J.3
  • 4
    • 15044349057 scopus 로고    scopus 로고
    • Characterisation of Aspergillus niger prolyl aminopeptidase
    • Basten, D. E., Moers, A. P., Ooyen, A. J. & Schaap, P. J. (2005). Characterisation of Aspergillus niger prolyl aminopeptidase. Mol Genet Genomics 272, 673-679.
    • (2005) Mol Genet Genomics , vol.272 , pp. 673-679
    • Basten, D.E.1    Moers, A.P.2    Ooyen, A.J.3    Schaap, P.J.4
  • 5
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J. D., Nielsen, H., von Heijne, G. & Brunak, S. (2004). Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340, 783-795.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 6
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A. & Weinstein, D. (1976). Assay of proteins in the presence of interfering materials. Anal Biochem 70, 241-250.
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 7
    • 0037224855 scopus 로고    scopus 로고
    • Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii
    • Bolumar, T., Sanz, Y., Aristoy, M. C. & Toldra, F. (2003). Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii. Appl Environ Microbiol 69, 227-232.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 227-232
    • Bolumar, T.1    Sanz, Y.2    Aristoy, M.C.3    Toldra, F.4
  • 9
    • 41349123095 scopus 로고    scopus 로고
    • Cellulases of mesophilic microorganisms: Cellulosome and noncellulosome producers
    • Doi, R. H. (2008). Cellulases of mesophilic microorganisms: cellulosome and noncellulosome producers. Ann N Y Acad Sci 1125, 267-279.
    • (2008) Ann N Y Acad Sci , vol.1125 , pp. 267-279
    • Doi, R.H.1
  • 10
    • 21644441527 scopus 로고    scopus 로고
    • Felipe, M. S., Andrade, R. V., Arraes, F. B., Nicola, A. M., Maranhão, A. Q., Torres, F. A., Silva-Pereira, I., Poc, as-Fonseca, M. J., Campos, E. G. & other authors (2005). Transcriptional profiles of the human pathogenic fungus Paracoccidioides brasiliensis in mycelium and yeast cells. J Biol Chem 280, 24706-24714.
    • Felipe, M. S., Andrade, R. V., Arraes, F. B., Nicola, A. M., Maranhão, A. Q., Torres, F. A., Silva-Pereira, I., Poc, as-Fonseca, M. J., Campos, E. G. & other authors (2005). Transcriptional profiles of the human pathogenic fungus Paracoccidioides brasiliensis in mycelium and yeast cells. J Biol Chem 280, 24706-24714.
  • 11
    • 1842530537 scopus 로고    scopus 로고
    • Carbon and nitrogen sources modulate lipase production in the yeast Yarrowia lipolytica
    • Fickers, P., Nicaud, J. M., Gaillardin, C., Destain, J. & Thonart, P. (2004). Carbon and nitrogen sources modulate lipase production in the yeast Yarrowia lipolytica. J Appl Microbiol 96, 742-749.
    • (2004) J Appl Microbiol , vol.96 , pp. 742-749
    • Fickers, P.1    Nicaud, J.M.2    Gaillardin, C.3    Destain, J.4    Thonart, P.5
  • 12
    • 21144478100 scopus 로고
    • The purification and characterization of prolyl aminopeptidase from Penicillium camemberti
    • Fuke, Y. & Matsuoka, H. (1993). The purification and characterization of prolyl aminopeptidase from Penicillium camemberti. J Dairy Sci 76, 2478-2484.
    • (1993) J Dairy Sci , vol.76 , pp. 2478-2484
    • Fuke, Y.1    Matsuoka, H.2
  • 13
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii
    • Grassick, A., Murray, P. G., Thompson, R., Collins, C. M., Byrnes, L., Birrane, G., Higgins, T. M. & Tuohy, M. G. (2004). Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Eur J Biochem 271, 4495-4506.
    • (2004) Eur J Biochem , vol.271 , pp. 4495-4506
    • Grassick, A.1    Murray, P.G.2    Thompson, R.3    Collins, C.M.4    Byrnes, L.5    Birrane, G.6    Higgins, T.M.7    Tuohy, M.G.8
  • 14
    • 34548463377 scopus 로고    scopus 로고
    • Cloning, characterisation and expression analysis of α-glucuronidase from the thermophilic fungus Talaromyces emersonii
    • Heneghan, M. N., McLoughlin, L., Murray, P. G. & Tuohy, M. G. (2007). Cloning, characterisation and expression analysis of α-glucuronidase from the thermophilic fungus Talaromyces emersonii. Enzyme Microb Technol 41, 677-682.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 677-682
    • Heneghan, M.N.1    McLoughlin, L.2    Murray, P.G.3    Tuohy, M.G.4
  • 16
    • 0042168991 scopus 로고    scopus 로고
    • Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor
    • Inoue, T., Ito, K., Tozaka, T., Hatakeyama, S., Tanaka, N., Nakamura, K. T. & Yoshimoto, T. (2003). Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor. Arch Biochem Biophys 416, 147-154.
    • (2003) Arch Biochem Biophys , vol.416 , pp. 147-154
    • Inoue, T.1    Ito, K.2    Tozaka, T.3    Hatakeyama, S.4    Tanaka, N.5    Nakamura, K.T.6    Yoshimoto, T.7
  • 18
    • 44949218553 scopus 로고    scopus 로고
    • In-gel digestion of proteins for MALDI-MS fingerprint mapping. Curr Protoc Protein Sci
    • Unit 16.4
    • Jiménez, C. R., Huang, L., Qiu, Y. & Burlingame, A. L. (2001). In-gel digestion of proteins for MALDI-MS fingerprint mapping. Curr Protoc Protein Sci Chapter 16, Unit 16.4.
    • (2001) Chapter , vol.16
    • Jiménez, C.R.1    Huang, L.2    Qiu, Y.3    Burlingame, A.L.4
  • 19
    • 0036939622 scopus 로고    scopus 로고
    • Isomaltose formed by α-glucosidases triggers amylase induction in Aspergillus nidulans
    • Kato, N., Murakoshi, Y., Kato, M., Kobayashi, T. & Tsukagoshi, N. (2002). Isomaltose formed by α-glucosidases triggers amylase induction in Aspergillus nidulans. Curr Genet 42, 43-50.
    • (2002) Curr Genet , vol.42 , pp. 43-50
    • Kato, N.1    Murakoshi, Y.2    Kato, M.3    Kobayashi, T.4    Tsukagoshi, N.5
  • 20
    • 0030001703 scopus 로고    scopus 로고
    • Prolyl aminopeptidase is also present in Enterobacteriaceae: Cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme
    • Kitazono, A., Kitano, A., Kabashima, T., Ito, K. & Yoshimoto, T. (1996). Prolyl aminopeptidase is also present in Enterobacteriaceae: cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme. J Biochem 119, 468-474.
    • (1996) J Biochem , vol.119 , pp. 468-474
    • Kitazono, A.1    Kitano, A.2    Kabashima, T.3    Ito, K.4    Yoshimoto, T.5
  • 22
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M. A, Blackshields, G, Brown, N. P, Chenna, R, McGettigan, P. A, McWilliam, H, Valentin, F, Wallace, I. M, Wilm, A. & other authors 2007, CLUSTAL W and CLUSTAL_X version 2.0. Bioinformatics 23, 2947-2948
    • Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A. & other authors (2007). CLUSTAL W and CLUSTAL_X version 2.0. Bioinformatics 23, 2947-2948.
  • 23
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K. & Jones, D. T. (2000). The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 24
    • 0032472380 scopus 로고    scopus 로고
    • Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: A prototype for the prolyl oligopeptidase family
    • Medrano, F. J., Alonso, J., Garcia, J. L., Romero, A., Bode, W. & Gomis-Ruth, F. X. (1998). Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family. EMBO J 17, 1-9.
    • (1998) EMBO J , vol.17 , pp. 1-9
    • Medrano, F.J.1    Alonso, J.2    Garcia, J.L.3    Romero, A.4    Bode, W.5    Gomis-Ruth, F.X.6
  • 25
    • 0035165769 scopus 로고    scopus 로고
    • Unusual susceptibility of a multidrug-resistant yeast strain to peptidic antifungals
    • Milewski, S., Mignini, F., Prasad, R. & Borowski, E. (2001). Unusual susceptibility of a multidrug-resistant yeast strain to peptidic antifungals. Antimicrob Agents Chemother 45, 223-228.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 223-228
    • Milewski, S.1    Mignini, F.2    Prasad, R.3    Borowski, E.4
  • 26
    • 16344394395 scopus 로고    scopus 로고
    • Identification of the reactive cysteine residues in oligopeptidase B from Trypanosoma brucei
    • Morty, R. E., Shih, A. Y., Fulop, V. & Andrews, N. W. (2005). Identification of the reactive cysteine residues in oligopeptidase B from Trypanosoma brucei. FEBS Lett 579, 2191-2196.
    • (2005) FEBS Lett , vol.579 , pp. 2191-2196
    • Morty, R.E.1    Shih, A.Y.2    Fulop, V.3    Andrews, N.W.4
  • 27
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-beta-glucanase active on 1,3-1,4-beta-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • Murray, P. G., Grassick, A., Laffey, C. D., Cuffe, M. M., Higgins, T., Savage, A. V., Planas, A. & Tuohy, M. G. (2001). Isolation and characterization of a thermostable endo-beta-glucanase active on 1,3-1,4-beta-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microb Technol 29, 90-98.
    • (2001) Enzyme Microb Technol , vol.29 , pp. 90-98
    • Murray, P.G.1    Grassick, A.2    Laffey, C.D.3    Cuffe, M.M.4    Higgins, T.5    Savage, A.V.6    Planas, A.7    Tuohy, M.G.8
  • 28
    • 0037423685 scopus 로고    scopus 로고
    • Molecular cloning, transcriptional, and expression analysis of the first cellulase gene (cbh2), encoding cellobiohydrolase II, from the moderately thermophilic fungus Talaromyces emersonii and structure prediction of the gene product
    • Murray, P. G., Collins, C. M., Grassick, A. & Tuohy, M. G. (2003). Molecular cloning, transcriptional, and expression analysis of the first cellulase gene (cbh2), encoding cellobiohydrolase II, from the moderately thermophilic fungus Talaromyces emersonii and structure prediction of the gene product. Biochem Biophys Res Commun 301, 280-286.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 280-286
    • Murray, P.G.1    Collins, C.M.2    Grassick, A.3    Tuohy, M.G.4
  • 33
    • 0022206304 scopus 로고
    • Rapid preparation of DNA from filamentous fungi
    • Raeder, U. & Broda, P. (1985). Rapid preparation of DNA from filamentous fungi. Lett Appl Microbiol 1, 17-20.
    • (1985) Lett Appl Microbiol , vol.1 , pp. 17-20
    • Raeder, U.1    Broda, P.2
  • 34
    • 0037564363 scopus 로고    scopus 로고
    • Molecular characterisation and expression analysis of the first hemicellulase gene (bxl1) encoding β-xylosidase from the thermophilic fungus Talaromyces emersonii
    • Reen, F. J., Murray, P. G. & Tuohy, M. G. (2003). Molecular characterisation and expression analysis of the first hemicellulase gene (bxl1) encoding β-xylosidase from the thermophilic fungus Talaromyces emersonii. Biochem Biophys Res Commun 305, 579-585.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 579-585
    • Reen, F.J.1    Murray, P.G.2    Tuohy, M.G.3
  • 35
    • 38649100624 scopus 로고    scopus 로고
    • Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei)
    • Stricker, A. R., Mach, R. L. & de Graaff, L. H. (2008). Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei). Appl Microbiol Biotechnol 78, 211-220.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 211-220
    • Stricker, A.R.1    Mach, R.L.2    de Graaff, L.H.3
  • 36
    • 55649090079 scopus 로고    scopus 로고
    • Proline as a stress protectant in yeast: Physiological functions, metabolic regulations, and biotechnological applications
    • Takagi, H. (2008). Proline as a stress protectant in yeast: physiological functions, metabolic regulations, and biotechnological applications. Appl Microbiol Biotechnol 81, 211-223.
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 211-223
    • Takagi, H.1
  • 37
    • 0027526567 scopus 로고
    • The xylan-degrading enzyme system of Talaromyces emersonii: Novel enzymes with activity against aryl β-D-xylosides and unsubstituted xylans
    • Tuohy, M. G., Puls, J., Claeyssens, M., Vrsanska, M. & Coughlan, M. P. (1993). The xylan-degrading enzyme system of Talaromyces emersonii: novel enzymes with activity against aryl β-D-xylosides and unsubstituted xylans. Biochem J 290, 515-523.
    • (1993) Biochem J , vol.290 , pp. 515-523
    • Tuohy, M.G.1    Puls, J.2    Claeyssens, M.3    Vrsanska, M.4    Coughlan, M.P.5
  • 38
    • 0028575479 scopus 로고
    • Characterization of the individual components of the xylanolytic enzyme system of Talaromyces emersonii
    • Tuohy, M. G., Laffey, C. D. & Coughlan, M. P. (1994). Characterization of the individual components of the xylanolytic enzyme system of Talaromyces emersonii. Bioresour Technol 50, 37-42.
    • (1994) Bioresour Technol , vol.50 , pp. 37-42
    • Tuohy, M.G.1    Laffey, C.D.2    Coughlan, M.P.3
  • 40
    • 33846041078 scopus 로고    scopus 로고
    • The Universal Protein Resource
    • UniProt
    • UniProt (2007). The Universal Protein Resource. Nucleic Acids Res 35, D193-D197.
    • (2007) Nucleic Acids Res , vol.35
  • 41
    • 0030471078 scopus 로고    scopus 로고
    • An operon from Lactobacillus helveticus composed of a proline iminopeptidase gene (pepI) and two genes coding for putative members of the ABC transporter family of proteins
    • Varmanen, P., Rantanen, T. & Palva, A. (1996). An operon from Lactobacillus helveticus composed of a proline iminopeptidase gene (pepI) and two genes coding for putative members of the ABC transporter family of proteins. Microbiology 142, 3459-3468.
    • (1996) Microbiology , vol.142 , pp. 3459-3468
    • Varmanen, P.1    Rantanen, T.2    Palva, A.3
  • 42
    • 0034045641 scopus 로고    scopus 로고
    • Detection of proteolytic activity by fluorescent zymogram in-gel assays
    • Yasothornsrikul, S. & Hook, V. Y. (2000). Detection of proteolytic activity by fluorescent zymogram in-gel assays. Biotechniques 28, 1166-1173.
    • (2000) Biotechniques , vol.28 , pp. 1166-1173
    • Yasothornsrikul, S.1    Hook, V.Y.2
  • 44
    • 34250638945 scopus 로고    scopus 로고
    • A proline iminopeptidase gene upregulated in planta by a LuxR homologue is essential for pathogenicity of Xanthomonas campestris pv. campestris
    • Zhang, L., Jia, Y., Wang, L. & Fang, R. (2007). A proline iminopeptidase gene upregulated in planta by a LuxR homologue is essential for pathogenicity of Xanthomonas campestris pv. campestris. Mol Microbiol 65, 121-136.
    • (2007) Mol Microbiol , vol.65 , pp. 121-136
    • Zhang, L.1    Jia, Y.2    Wang, L.3    Fang, R.4


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