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Volumn 25, Issue 4, 2011, Pages 165-171

Sensory perception in fungal pathogens: Applications of the split-ubiquitin Membrane Yeast Two-Hybrid (MYTH) technique

Author keywords

A. fumigatus; Membrane Yeast Two Hybrid assay; PH sensing; Protein protein interactions; Split ubiquitin

Indexed keywords

ASPERGILLUS FUMIGATUS; FUNGI;

EID: 82455199241     PISSN: 17494613     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fbr.2011.10.002     Document Type: Review
Times cited : (3)

References (53)
  • 1
    • 66449127673 scopus 로고    scopus 로고
    • Systemic analysis of the response of Aspergillus niger to ambient pH
    • Andersen M., Lehmann L., Nielsen J. Systemic analysis of the response of Aspergillus niger to ambient pH. Genome Biol. 2009, 10:R47.
    • (2009) Genome Biol. , vol.10
    • Andersen, M.1    Lehmann, L.2    Nielsen, J.3
  • 2
    • 0035987407 scopus 로고    scopus 로고
    • The post-genomic era of interactive proteomics: facts and perspectives
    • Auerbach D., Thaminy S., Hottiger M.O., Stagljar I. The post-genomic era of interactive proteomics: facts and perspectives. Proteomics 2002, 2:611-623.
    • (2002) Proteomics , vol.2 , pp. 611-623
    • Auerbach, D.1    Thaminy, S.2    Hottiger, M.O.3    Stagljar, I.4
  • 6
    • 0035823039 scopus 로고    scopus 로고
    • Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease
    • Cervantes S., Gonzalez-Duarte R., Marfany G. Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease. FEBS Lett. 2001, 505:81-86.
    • (2001) FEBS Lett. , vol.505 , pp. 81-86
    • Cervantes, S.1    Gonzalez-Duarte, R.2    Marfany, G.3
  • 7
    • 0030659412 scopus 로고    scopus 로고
    • In vitro susceptibility of respiratory isolates of Aspergillus species to itraconazole and amphotericin B acquired resistance to itraconazole
    • Chryssanthou E. In vitro susceptibility of respiratory isolates of Aspergillus species to itraconazole and amphotericin B acquired resistance to itraconazole. Scand. J. Infect. Dis. 1997, 29:509-512.
    • (1997) Scand. J. Infect. Dis. , vol.29 , pp. 509-512
    • Chryssanthou, E.1
  • 8
    • 0142092728 scopus 로고    scopus 로고
    • Adaptation to environmental pH in Candida albicans and its relation to pathogenesis
    • Davis D. Adaptation to environmental pH in Candida albicans and its relation to pathogenesis. Curr. Genet. 2003, 44:1-7.
    • (2003) Curr. Genet. , vol.44 , pp. 1-7
    • Davis, D.1
  • 9
    • 0033796715 scopus 로고    scopus 로고
    • Candida albicans RIM101 pH response pathway is required for host-pathogen interactions
    • Davis D., Edwards J.E., Mitchell A.P., Ibrahim A.S. Candida albicans RIM101 pH response pathway is required for host-pathogen interactions. Infect. Immun. 2000, 68:5953-5959.
    • (2000) Infect. Immun. , vol.68 , pp. 5953-5959
    • Davis, D.1    Edwards, J.E.2    Mitchell, A.P.3    Ibrahim, A.S.4
  • 10
    • 2642632760 scopus 로고    scopus 로고
    • The pH of the host niche controls gene expression in and virulence of Candida albicans
    • De Bernardis F., Muhlschlegel F.A., Cassone A., Fonzi W.A. The pH of the host niche controls gene expression in and virulence of Candida albicans. Infect. Immun. 1998, 66:3317-3325.
    • (1998) Infect. Immun. , vol.66 , pp. 3317-3325
    • De Bernardis, F.1    Muhlschlegel, F.A.2    Cassone, A.3    Fonzi, W.A.4
  • 11
    • 0028892964 scopus 로고
    • Signaling of ambient pH in Aspergillus involves a cysteine protease
    • Denison S., Orejas M., Arst H. Signaling of ambient pH in Aspergillus involves a cysteine protease. J. Biol. Chem. 1995, 270:28519.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28519
    • Denison, S.1    Orejas, M.2    Arst, H.3
  • 13
    • 0030824612 scopus 로고    scopus 로고
    • Correlation between in-vitro susceptibility testing to itraconazole and in-vivo outcome of Aspergillus fumigatus infection
    • Denning D.W., Radford S.A., Oakley K.L., Hall L., Johnson E.M., Warnock D.W. Correlation between in-vitro susceptibility testing to itraconazole and in-vivo outcome of Aspergillus fumigatus infection. J. Antimicrob. Chemother. 1997, 40:401-414.
    • (1997) J. Antimicrob. Chemother. , vol.40 , pp. 401-414
    • Denning, D.W.1    Radford, S.A.2    Oakley, K.L.3    Hall, L.4    Johnson, E.M.5    Warnock, D.W.6
  • 15
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protoc. 2007, 2:953-971.
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 16
    • 70849110573 scopus 로고    scopus 로고
    • Infectious diseases. Farm fungicides linked to resistance in a human pathogen
    • Enserink M. Infectious diseases. Farm fungicides linked to resistance in a human pathogen. Science 2009, 326:1173.
    • (2009) Science , vol.326 , pp. 1173
    • Enserink, M.1
  • 17
    • 33750466866 scopus 로고    scopus 로고
    • The pH signaling transcription factor PacC mediates the growth of Trichophyton rubrum on human nail in vitro
    • Ferreira-Nozawa M.S., Silveira H.C., Ono C.J., Fachin A.L., Rossi A., Martinez-Rossi N.M. The pH signaling transcription factor PacC mediates the growth of Trichophyton rubrum on human nail in vitro. Med. Mycol. 2006, 44:641-645.
    • (2006) Med. Mycol. , vol.44 , pp. 641-645
    • Ferreira-Nozawa, M.S.1    Silveira, H.C.2    Ono, C.J.3    Fachin, A.L.4    Rossi, A.5    Martinez-Rossi, N.M.6
  • 18
    • 1542285258 scopus 로고    scopus 로고
    • Application of the split-ubiquitin membrane yeast two-hybrid system to investigate membrane protein interactions
    • Fetchko M., Stagljar I. Application of the split-ubiquitin membrane yeast two-hybrid system to investigate membrane protein interactions. Methods 2004, 32:349-362.
    • (2004) Methods , vol.32 , pp. 349-362
    • Fetchko, M.1    Stagljar, I.2
  • 19
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature 1989, 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 20
    • 0035984722 scopus 로고    scopus 로고
    • β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau A., Primeau M., Trudeau L.E., Michnick S.W. β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol. 2002, 20:619-622.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 22
    • 47849096465 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions between the mammalian integral membrane transporters and PDZ-interacting partners using a modified split-ubiquitin membrane yeast two-hybrid system
    • Gisler S.M., Kittanakom S., Fuster D., Wong V., Bertic M., Radanovic T., Hall R.A., Murer H., Biber J., Markovich D., Moe O.W., Stagljar I. Monitoring protein-protein interactions between the mammalian integral membrane transporters and PDZ-interacting partners using a modified split-ubiquitin membrane yeast two-hybrid system. Mol. Cell. Proteomics 2008, 7:1362-1377.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1362-1377
    • Gisler, S.M.1    Kittanakom, S.2    Fuster, D.3    Wong, V.4    Bertic, M.5    Radanovic, T.6    Hall, R.A.7    Murer, H.8    Biber, J.9    Markovich, D.10    Moe, O.W.11    Stagljar, I.12
  • 24
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992, 61:761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 26
    • 33644874395 scopus 로고    scopus 로고
    • Utilizing the split-ubiquitin membrane yeast two-hybrid system to identify protein-protein interactions of integral membrane proteins
    • Iyer K., Burkle L., Auerbach D., Thaminy S., Dinkel M., Engels K., Stagljar I. Utilizing the split-ubiquitin membrane yeast two-hybrid system to identify protein-protein interactions of integral membrane proteins. Sci. Signal. 2005, 2005.
    • (2005) Sci. Signal. , vol.2005
    • Iyer, K.1    Burkle, L.2    Auerbach, D.3    Thaminy, S.4    Dinkel, M.5    Engels, K.6    Stagljar, I.7
  • 27
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson N., Varshavsky A. Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl. Acad. Sci. 1994, 91:10340.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 10340
    • Johnsson, N.1    Varshavsky, A.2
  • 29
    • 0342460608 scopus 로고    scopus 로고
    • The sequence of palF, an environmental pH response gene in Aspergillus nidulans
    • Maccheroni W., May G.S., Martinez-Rossi N.M., Rossi A. The sequence of palF, an environmental pH response gene in Aspergillus nidulans. Gene 1997, 194:163-167.
    • (1997) Gene , vol.194 , pp. 163-167
    • Maccheroni, W.1    May, G.S.2    Martinez-Rossi, N.M.3    Rossi, A.4
  • 30
    • 0035697120 scopus 로고    scopus 로고
    • Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system
    • Massaad M.J., Herscovics A. Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. J. Cell Sci. 2001, 114:4629-4635.
    • (2001) J. Cell Sci. , vol.114 , pp. 4629-4635
    • Massaad, M.J.1    Herscovics, A.2
  • 32
    • 0031038837 scopus 로고    scopus 로고
    • Characterization of the pH signal transduction pathway gene palA of Aspergillus nidulans and identification of possible homologs
    • Negrete-Urtasun S., Denison S.H., Arst H.N. Characterization of the pH signal transduction pathway gene palA of Aspergillus nidulans and identification of possible homologs. J. Bacteriol. 1997, 179:1832-1835.
    • (1997) J. Bacteriol. , vol.179 , pp. 1832-1835
    • Negrete-Urtasun, S.1    Denison, S.H.2    Arst, H.N.3
  • 36
    • 9244245261 scopus 로고    scopus 로고
    • Recent advances in the characterization of ambient pH regulation of gene expression in filamentous fungi and yeasts
    • Peñalva M., Arst H. Recent advances in the characterization of ambient pH regulation of gene expression in filamentous fungi and yeasts. Annu. Rev. Microbiol. 2004, 58:425-451.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 425-451
    • Peñalva, M.1    Arst, H.2
  • 37
    • 44949242315 scopus 로고    scopus 로고
    • Ambient pH gene regulation in fungi: making connections
    • Peñalva M., Tilburn J., Bignell E., Arst H. Ambient pH gene regulation in fungi: making connections. Trends Microbiol. 2008, 16:291-300.
    • (2008) Trends Microbiol. , vol.16 , pp. 291-300
    • Peñalva, M.1    Tilburn, J.2    Bignell, E.3    Arst, H.4
  • 38
    • 0036284612 scopus 로고    scopus 로고
    • Intra- and intermolecular interactions in sucrose transporters at the plasma membrane detected by the split-ubiquitin system and functional assays
    • Reinders A., Schulze W., Thaminy S., Stagljar I., Frommer W.B., Ward J.M. Intra- and intermolecular interactions in sucrose transporters at the plasma membrane detected by the split-ubiquitin system and functional assays. Structure 2002, 10:763-772.
    • (2002) Structure , vol.10 , pp. 763-772
    • Reinders, A.1    Schulze, W.2    Thaminy, S.3    Stagljar, I.4    Frommer, W.B.5    Ward, J.M.6
  • 39
    • 0035575637 scopus 로고    scopus 로고
    • Drug discovery of the future: the implications of the human genome project
    • Reiss T. Drug discovery of the future: the implications of the human genome project. Trends Biotechnol. 2001, 19:496-499.
    • (2001) Trends Biotechnol. , vol.19 , pp. 496-499
    • Reiss, T.1
  • 40
    • 63249101831 scopus 로고    scopus 로고
    • Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III
    • Rodriguez-Galan O., Galindo A., Hervas-Aguilar A., Arst H.N., Penalva M.A. Physiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III. J. Biol. Chem. 2009, 284:4404-4412.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4404-4412
    • Rodriguez-Galan, O.1    Galindo, A.2    Hervas-Aguilar, A.3    Arst, H.N.4    Penalva, M.A.5
  • 41
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation
    • Rossi F., Charlton C.A., Blau H.M. Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:8405-8410.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 42
    • 0141733061 scopus 로고    scopus 로고
    • Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein
    • Scheper W., Thaminy S., Kais S., Stagljar I., Römisch K. Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein. J. Biol. Chem. 2003, 278:37998-38003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37998-38003
    • Scheper, W.1    Thaminy, S.2    Kais, S.3    Stagljar, I.4    Römisch, K.5
  • 43
    • 80055113163 scopus 로고    scopus 로고
    • Split-ubiquitin based membrane yeast two-hybrid (MYTH) system: a powerful tool for identifying protein-protein interactions
    • Snider J., Kittanakom S., Curak J., Stagljar I. Split-ubiquitin based membrane yeast two-hybrid (MYTH) system: a powerful tool for identifying protein-protein interactions. J. Vis. Exp. 2010.
    • (2010) J. Vis. Exp.
    • Snider, J.1    Kittanakom, S.2    Curak, J.3    Stagljar, I.4
  • 44
    • 77954249974 scopus 로고    scopus 로고
    • Detecting interactions with membrane proteins using a membrane two-hybrid assay in yeast
    • Snider J., Kittanakom S., Damjanovic D., Curak J., Wong V., Stagljar I. Detecting interactions with membrane proteins using a membrane two-hybrid assay in yeast. Nat. Protoc. 2010, 5:1281-1293.
    • (2010) Nat. Protoc. , vol.5 , pp. 1281-1293
    • Snider, J.1    Kittanakom, S.2    Damjanovic, D.3    Curak, J.4    Wong, V.5    Stagljar, I.6
  • 45
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar I., Korostensky C., Johnsson N., Te Heesen S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:5187.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5187
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    Te Heesen, S.4
  • 46
    • 0027230493 scopus 로고
    • The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis
    • Tang C.M., Cohen J., Krausz T., Van Noorden S., Holden D.W. The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect. Immun. 1993, 61:1650-1656.
    • (1993) Infect. Immun. , vol.61 , pp. 1650-1656
    • Tang, C.M.1    Cohen, J.2    Krausz, T.3    Van Noorden, S.4    Holden, D.W.5
  • 47
    • 0037810425 scopus 로고    scopus 로고
    • Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system
    • Thaminy S., Auerbach D., Arnoldo A., Stagljar I. Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system. Genome Res. 2003, 13:1744-1753.
    • (2003) Genome Res. , vol.13 , pp. 1744-1753
    • Thaminy, S.1    Auerbach, D.2    Arnoldo, A.3    Stagljar, I.4
  • 48
    • 0031977161 scopus 로고    scopus 로고
    • Efficacy of LY303366 against amphotericin B-susceptible and -resistant Aspergillus fumigatus in a murine model of invasive aspergillosis
    • Verweij P.E., Oakley K.L., Morrissey J., Morrissey G., Denning D.W. Efficacy of LY303366 against amphotericin B-susceptible and -resistant Aspergillus fumigatus in a murine model of invasive aspergillosis. Antimicrob. Agents Chemother. 1998, 42:873-878.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 873-878
    • Verweij, P.E.1    Oakley, K.L.2    Morrissey, J.3    Morrissey, G.4    Denning, D.W.5
  • 49
    • 71549143158 scopus 로고    scopus 로고
    • Azole resistance in Aspergillus fumigatus: a side-effect of environmental fungicide use?
    • Verweij P.E., Snelders E., Kema G.H., Mellado E., Melchers W.J. Azole resistance in Aspergillus fumigatus: a side-effect of environmental fungicide use?. Lancet Infect. Dis. 2009, 9:789-795.
    • (2009) Lancet Infect. Dis. , vol.9 , pp. 789-795
    • Verweij, P.E.1    Snelders, E.2    Kema, G.H.3    Mellado, E.4    Melchers, W.J.5
  • 50
    • 67650635116 scopus 로고    scopus 로고
    • Roles of the pH signaling transcription factor PacC in Wangiella (Exophiala) dermatitidis
    • Wang Q., Szaniszlo P.J. Roles of the pH signaling transcription factor PacC in Wangiella (Exophiala) dermatitidis. Fungal Genet. Biol. 2009, 46:657-666.
    • (2009) Fungal Genet. Biol. , vol.46 , pp. 657-666
    • Wang, Q.1    Szaniszlo, P.J.2
  • 51
    • 1642265742 scopus 로고    scopus 로고
    • The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B
    • Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C. The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B. Mol. Cell. Biol. 2004, 24:2767-2778.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2767-2778
    • Wang, B.1    Pelletier, J.2    Massaad, M.J.3    Herscovics, A.4    Shore, G.C.5
  • 52
    • 34548022105 scopus 로고    scopus 로고
    • The Colletotrichum acutatum gene encoding a putative pH-responsive transcription regulator is a key virulence determinant during fungal pathogenesis on citrus
    • You B.J., Choquer M., Chung K.R. The Colletotrichum acutatum gene encoding a putative pH-responsive transcription regulator is a key virulence determinant during fungal pathogenesis on citrus. Mol. Plant Microbe Interact. 2007, 20:1149-1160.
    • (2007) Mol. Plant Microbe Interact. , vol.20 , pp. 1149-1160
    • You, B.J.1    Choquer, M.2    Chung, K.R.3
  • 53
    • 78049438537 scopus 로고    scopus 로고
    • PacC in the nematophagous fungus Clonostachys rosea controls virulence to nematodes
    • Zou C.G., Tu H.H., Liu X.Y., Tao N., Zhang K.Q. PacC in the nematophagous fungus Clonostachys rosea controls virulence to nematodes. Environ. Microbiol. 2010, 12:1868-1877.
    • (2010) Environ. Microbiol. , vol.12 , pp. 1868-1877
    • Zou, C.G.1    Tu, H.H.2    Liu, X.Y.3    Tao, N.4    Zhang, K.Q.5


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