메뉴 건너뛰기




Volumn 30, Issue 2, 2013, Pages 183-191

Stress effects caused by the expression of a mutant cellobiohydrolase I and proteasome inhibition in Trichoderma reesei Rut-C30

Author keywords

[No Author keywords available]

Indexed keywords

CELLOBIOHYDROLASE I; CELLULAR EFFECTS; CONFOCAL FLUORESCENCE MICROSCOPY; CONFOCAL LASER SCANNING MICROSCOPY; DNA ENCODING; ER STRESS; FILAMENTOUS FUNGI; FUNGAL HYPHAE; FUSION PROTEINS; GENE PRODUCTS; MISFOLDED PROTEINS; PROTEASOMES; PROTEIN QUALITY CONTROL; PROTEIN SECRETION; PROTEIN YIELD; Q-RT-PCR; SECRETED PROTEIN; STRESS EFFECTS; SUBCELLULAR LOCATION; T. REESEI; TRICHODERMA REESEI; UP-REGULATION;

EID: 84872391082     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2012.07.005     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 42549105668 scopus 로고    scopus 로고
    • Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview
    • Gasser B., et al. Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview. Microb. Cell Fact. 2008, 7:11-29.
    • (2008) Microb. Cell Fact. , vol.7 , pp. 11-29
    • Gasser, B.1
  • 3
    • 34249749971 scopus 로고    scopus 로고
    • Heterologous gene expression in filamentous fungi - a holistic view
    • Elsevier Science BV, D.K. Arora, G.G. Kchachatourians (Eds.)
    • Nevalainen H., et al. Heterologous gene expression in filamentous fungi - a holistic view. Applied Mycology & Biotechnology. An International Series. Volume 5, Genes and Genomics 2005, 211-237. Elsevier Science BV. D.K. Arora, G.G. Kchachatourians (Eds.).
    • (2005) Applied Mycology & Biotechnology. An International Series. Volume 5, Genes and Genomics , pp. 211-237
    • Nevalainen, H.1
  • 4
    • 84855228527 scopus 로고    scopus 로고
    • Trichoderma reesei RUT-C30 - thirty years of strain improvement
    • Peterson R., Nevalainen H. Trichoderma reesei RUT-C30 - thirty years of strain improvement. Microbiology 2012, 158:58-68.
    • (2012) Microbiology , vol.158 , pp. 58-68
    • Peterson, R.1    Nevalainen, H.2
  • 5
    • 48249114001 scopus 로고    scopus 로고
    • The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85kb (29 gene-encoding) region of the wild-type genome
    • Seidl V., et al. The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85kb (29 gene-encoding) region of the wild-type genome. BMC Genom. 2008, 9:327-342.
    • (2008) BMC Genom. , vol.9 , pp. 327-342
    • Seidl, V.1
  • 7
    • 70349482673 scopus 로고    scopus 로고
    • Tracking the roots of cellulase hyperproduction by the fungus Trichoderma reesei using massively parallel DNA sequencing
    • Le Crom S., et al. Tracking the roots of cellulase hyperproduction by the fungus Trichoderma reesei using massively parallel DNA sequencing. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:16151-16156.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16151-16156
    • Le Crom, S.1
  • 8
    • 0020102765 scopus 로고
    • Increased endoplasmic reticulum content of a mutant of Trichoderma reesei (RUT-C30) in relation to cellulase synthesis
    • Ghosh A., et al. Increased endoplasmic reticulum content of a mutant of Trichoderma reesei (RUT-C30) in relation to cellulase synthesis. Enzyme Microb. Technol. 1982, 4:110-113.
    • (1982) Enzyme Microb. Technol. , vol.4 , pp. 110-113
    • Ghosh, A.1
  • 9
    • 0021680425 scopus 로고
    • Cellulase secretion from a hyper-cellulolytic mutant of Trichoderma reesei RUT-C30
    • Ghosh A., et al. Cellulase secretion from a hyper-cellulolytic mutant of Trichoderma reesei RUT-C30. Arch. Microbiol. 1984, 140:126-133.
    • (1984) Arch. Microbiol. , vol.140 , pp. 126-133
    • Ghosh, A.1
  • 10
    • 0037323934 scopus 로고    scopus 로고
    • Activation mechanisms of the HAC1-mediated unfolded protein response in filamentous fungi
    • Saloheimo M., et al. Activation mechanisms of the HAC1-mediated unfolded protein response in filamentous fungi. Mol. Microbiol. 2003, 47:1149-1161.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1149-1161
    • Saloheimo, M.1
  • 11
    • 11244353370 scopus 로고    scopus 로고
    • The ire1 and ptc2 genes involved in the unfolded protein response pathway in the filamentous fungus Trichoderma reesei
    • Valkonen M., et al. The ire1 and ptc2 genes involved in the unfolded protein response pathway in the filamentous fungus Trichoderma reesei. Mol. Gen. Genomics 2004, 272:443-451.
    • (2004) Mol. Gen. Genomics , vol.272 , pp. 443-451
    • Valkonen, M.1
  • 12
    • 0242581693 scopus 로고    scopus 로고
    • The effects of drugs inhibiting protein secretion in the filamentous fungus Trichoderma reesei
    • Pakula T.M., et al. The effects of drugs inhibiting protein secretion in the filamentous fungus Trichoderma reesei. J. Biol. Chem. 2003, 278:45011-45020.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45011-45020
    • Pakula, T.M.1
  • 13
    • 84855217145 scopus 로고    scopus 로고
    • The cargo and the transport system: secreted proteins and protein secretion in Trichoderma reesei (Hypocrea jecorina)
    • Saloheimo M., Pakula T.M. The cargo and the transport system: secreted proteins and protein secretion in Trichoderma reesei (Hypocrea jecorina). Microbiology 2012, 158:46-57.
    • (2012) Microbiology , vol.158 , pp. 46-57
    • Saloheimo, M.1    Pakula, T.M.2
  • 14
    • 33845399098 scopus 로고    scopus 로고
    • The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins
    • Goffin L., et al. The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins. Mol. Biol. Cell 2006, 17:5309-5323.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5309-5323
    • Goffin, L.1
  • 15
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signalling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals
    • Patil C., Walter P. Intracellular signalling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 2001, 13:349-355.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 16
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: on protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 1998, 15:7151-7160.
    • (1998) EMBO J. , vol.15 , pp. 7151-7160
    • Ciechanover, A.1
  • 17
    • 18444378154 scopus 로고    scopus 로고
    • Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo
    • Sims A.H., et al. Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo. Appl. Environ. Microbiol. 2005, 71:2737-2747.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2737-2747
    • Sims, A.H.1
  • 19
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M., et al. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 1997, 16:4540-4548.
    • (1997) EMBO J. , vol.16 , pp. 4540-4548
    • Pilon, M.1
  • 20
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • Nakatsukasa K., Brodsky J.L. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 2008, 9:861-870.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 21
    • 64549115746 scopus 로고    scopus 로고
    • Toward an atomic model of the 26S proteasome
    • Cheng Y. Toward an atomic model of the 26S proteasome. Curr. Opin. Struct. Biol. 2009, 14:203-208.
    • (2009) Curr. Opin. Struct. Biol. , vol.14 , pp. 203-208
    • Cheng, Y.1
  • 22
    • 21144450049 scopus 로고    scopus 로고
    • ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle
    • Babbit S.E., et al. ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle. Cell 2005, 121:552-565.
    • (2005) Cell , vol.121 , pp. 552-565
    • Babbit, S.E.1
  • 23
    • 0031922043 scopus 로고    scopus 로고
    • Trichoderma reesei prs12 encodes a stress - and unfolded-protein-response-inducible regulatory subunit of the fungal 26S proteasome
    • Goller S.P., et al. Trichoderma reesei prs12 encodes a stress - and unfolded-protein-response-inducible regulatory subunit of the fungal 26S proteasome. Curr. Genet. 1998, 33:284-290.
    • (1998) Curr. Genet. , vol.33 , pp. 284-290
    • Goller, S.P.1
  • 24
    • 33846414684 scopus 로고    scopus 로고
    • Proteome mapping of the Trichoderma reesei 20S proteasome
    • Grinyer J., et al. Proteome mapping of the Trichoderma reesei 20S proteasome. Curr. Genet. 2007, 51:79-88.
    • (2007) Curr. Genet. , vol.51 , pp. 79-88
    • Grinyer, J.1
  • 25
    • 67650108534 scopus 로고    scopus 로고
    • Nevalainen Rapid purification method for the 26S proteasome from the filamentous fungus Trichoderma reesei
    • Kautto L., et al. Nevalainen Rapid purification method for the 26S proteasome from the filamentous fungus Trichoderma reesei. Protein Expr. Purif. 2009, 67:156-163.
    • (2009) Protein Expr. Purif. , vol.67 , pp. 156-163
    • Kautto, L.1
  • 26
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee H.D., Goldberg A.L. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J. Biol. Chem. 1996, 271:27280-27284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, H.D.1    Goldberg, A.L.2
  • 27
    • 0023553310 scopus 로고
    • A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei
    • Penttilä M., et al. A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei. Gene 1987, 61:155-164.
    • (1987) Gene , vol.61 , pp. 155-164
    • Penttilä, M.1
  • 28
    • 0035406437 scopus 로고    scopus 로고
    • Proteins associated with the cell envelope of Trichoderma reesei: a proteomic approach
    • Lim D., et al. Proteins associated with the cell envelope of Trichoderma reesei: a proteomic approach. Proteomics 2001, 1:899-910.
    • (2001) Proteomics , vol.1 , pp. 899-910
    • Lim, D.1
  • 29
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T., et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1
  • 30
    • 0021078994 scopus 로고
    • Plasmid encoded hygromycin B resistance: the sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae
    • Gritz L., Davies J. Plasmid encoded hygromycin B resistance: the sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae. Gene 1983, 25:179-183.
    • (1983) Gene , vol.25 , pp. 179-183
    • Gritz, L.1    Davies, J.2
  • 31
    • 0027240523 scopus 로고
    • Characterization of the pyruvate kinase gene (pki1) of Trichoderma reesei
    • Schindler M., et al. Characterization of the pyruvate kinase gene (pki1) of Trichoderma reesei. Gene 1993, 130:271-275.
    • (1993) Gene , vol.130 , pp. 271-275
    • Schindler, M.1
  • 32
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., et al. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989, 1:51-59.
    • (1989) Gene , vol.1 , pp. 51-59
    • Ho, S.N.1
  • 33
    • 0034283706 scopus 로고    scopus 로고
    • Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus, Trichoderma reesei
    • Te'o V.S.J., et al. Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus, Trichoderma reesei. FEMS Microbiol. Lett. 2000, 190:13-19.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 13-19
    • Te'o, V.S.J.1
  • 34
    • 0002442188 scopus 로고
    • A rapid, high yield mini prep method for isolation of total genomic DNA from fungi
    • Lee S.B., et al. A rapid, high yield mini prep method for isolation of total genomic DNA from fungi. Fungal Genet Newsl. 1988, 35:23-24.
    • (1988) Fungal Genet Newsl. , vol.35 , pp. 23-24
    • Lee, S.B.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen S., Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. Methods Mol. Biol. 2000, 132:365-386.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 38
    • 67949120452 scopus 로고    scopus 로고
    • Microarray analysis of phosphate regulation in the marine cyanobacterium Synechococcus sp., WH8102
    • Tetu S.G., et al. Microarray analysis of phosphate regulation in the marine cyanobacterium Synechococcus sp., WH8102. ISME J. 2009, 3:835-849.
    • (2009) ISME J. , vol.3 , pp. 835-849
    • Tetu, S.G.1
  • 39
    • 33744981623 scopus 로고    scopus 로고
    • Image processing with ImageJ
    • Abramoff M.D., et al. Image processing with ImageJ. Biophoton. Intl. 2004, 11:36-42.
    • (2004) Biophoton. Intl. , vol.11 , pp. 36-42
    • Abramoff, M.D.1
  • 40
    • 44049083225 scopus 로고    scopus 로고
    • Fungal mycelia show lag time before re-growth on endogenous carbon
    • Pollack J.K., et al. Fungal mycelia show lag time before re-growth on endogenous carbon. Biotechnol. Bioeng. 2008, 100:458-465.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 458-465
    • Pollack, J.K.1
  • 41
    • 0028877138 scopus 로고
    • Production of recombinant proteins in the filamentous fungus Trichoderma reesei
    • Keränen S., Penttilä M. Production of recombinant proteins in the filamentous fungus Trichoderma reesei. Curr. Opin. Biotechnol. 1995, 6:534-537.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 534-537
    • Keränen, S.1    Penttilä, M.2
  • 42
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung J., et al. The ubiquitin-proteasome pathway and proteasome inhibitors. Med. Res. Rev. 2001, 21:245-273.
    • (2001) Med. Res. Rev. , vol.21 , pp. 245-273
    • Myung, J.1
  • 43
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schröder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 2008, 65:862-894.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 862-894
    • Schröder, M.1
  • 44
    • 33947301163 scopus 로고    scopus 로고
    • Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum
    • Ng W., et al. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J. Cell Sci. 2007, 120:682-691.
    • (2007) J. Cell Sci. , vol.120 , pp. 682-691
    • Ng, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.