메뉴 건너뛰기




Volumn 70, Issue 12, 2004, Pages 7530-7538

Analysis of proteasome-dependent proteolysis in Haloferax volcanii cells, using short-lived green fluorescent proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; FLUORESCENCE; FLUORINE; GENES; METHANE; PHENOLS;

EID: 10444253995     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.12.7530-7538.2004     Document Type: Article
Times cited : (69)

References (31)
  • 2
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., J. Walz, F. Zühl, and E. Seemüller. 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 3
    • 0033769733 scopus 로고    scopus 로고
    • PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
    • Benaroudj, N., and A. L. Goldberg. 2000. PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone. Nat. Cell Biol. 2:833-839.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 833-839
    • Benaroudj, N.1    Goldberg, A.L.2
  • 4
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj, N., P. Zwickl, E. Seemuller, W. Baumeister, and A. L. Goldberg. 2003. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11:69-78.
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemuller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 5
    • 0036092772 scopus 로고    scopus 로고
    • Proteasome inhibitors: Complex tools for a complex enzyme
    • Bogyo, M., and E. W. Wang. 2002. Proteasome inhibitors: complex tools for a complex enzyme. Curr. Top. Microbiol. Immunol. 268:185-208.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.268 , pp. 185-208
    • Bogyo, M.1    Wang, E.W.2
  • 6
    • 0035310832 scopus 로고    scopus 로고
    • Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling
    • Chiesa, A., E. Rapizzi, V. Tosello, P. Pinton, M. de Virgilio, K. E. Fogarty, and R. Rizzuto. 2001. Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling. Biochem. J. 355:1-12.
    • (2001) Biochem. J. , vol.355 , pp. 1-12
    • Chiesa, A.1    Rapizzi, E.2    Tosello, V.3    Pinton, P.4    De Virgilio, M.5    Fogarty, K.E.6    Rizzuto, R.7
  • 8
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., E. A. Whitehorn, E. Tate, and W. P. Stemmer. 1996. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14:315-319.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 9
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis, S. J., and R. D. Vierstra. 1998. Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol. Biol. 36:521-528.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 521-528
    • Davis, S.J.1    Vierstra, R.D.2
  • 10
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany, G., and S. L. Schreiber. 1998. Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273:8545-8548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 11
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 12
    • 0035845498 scopus 로고    scopus 로고
    • Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
    • Flynn, J. M., I. Levchenko, M. Seidel, S. H. Wickner, R. T. Sauer, and T. A. Baker. 2001. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. USA 98:10584-10589.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10584-10589
    • Flynn, J.M.1    Levchenko, I.2    Seidel, M.3    Wickner, S.H.4    Sauer, R.T.5    Baker, T.A.6
  • 13
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda, H., M. Arai, and K. Kuwajima. 2000. Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39:12025-12032.
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 14
    • 0032079329 scopus 로고    scopus 로고
    • The CIpXP and CIpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., E. Roche, Y. Zhou, and R. T. Sauer. 1998. The CIpXP and CIpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 16
    • 0030930383 scopus 로고    scopus 로고
    • Site-directed mutagenesis and halophilicity of dihydrolipoamide dehydrogenase from the halophilic archaeon, Haloferax volcanii
    • Jolley, K. A., R. J. Russell, D. W. Hough, and M. J. Danson. 1997. Site-directed mutagenesis and halophilicity of dihydrolipoamide dehydrogenase from the halophilic archaeon, Haloferax volcanii. Eur. J. Biochem. 248:362-368.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 362-368
    • Jolley, K.A.1    Russell, R.J.2    Hough, D.W.3    Danson, M.J.4
  • 17
    • 0037214430 scopus 로고    scopus 로고
    • Subunit topology of two 20S proteasomes from Haloferax volcanii
    • Kaczowka, S. J., and J. A. Maupin-Furlow. 2003. Subunit topology of two 20S proteasomes from Haloferax volcanii. J. Bacteriol. 185:165-174.
    • (2003) J. Bacteriol. , vol.185 , pp. 165-174
    • Kaczowka, S.J.1    Maupin-Furlow, J.A.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 21
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech, M., F. Frolow, and L. M. Gloss. 2000. Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86:155-164.
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 22
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon, A., and A. L. Goldberg. 2001. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8:1339-1349.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 23
    • 0031786572 scopus 로고    scopus 로고
    • Functional expression of green fluorescent protein derivatives in Halobacterium salinarum
    • Nomura, S., and Y. Harada. 1998. Functional expression of green fluorescent protein derivatives in Halobacterium salinarum. FEMS Microbiol. Lett. 167: 287-293.
    • (1998) FEMS Microbiol. Lett. , vol.167 , pp. 287-293
    • Nomura, S.1    Harada, Y.2
  • 24
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M., A. B. Cubitt, K. Kallio, L. A. Gross, R. Y. Tsien, and S. J. Remington. 1996. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273:1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 25
    • 7744243704 scopus 로고    scopus 로고
    • Differential regulation of the PanA and PanB proteasome-activating nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax volcanii
    • Reuter, C. J., S. J. Kaczowka, and J. A. Maupin-Furlow. 2004. Differential regulation of the PanA and PanB proteasome-activating nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax volcanii. J. Bacteriol. 186:7763-7772.
    • (2004) J. Bacteriol. , vol.186 , pp. 7763-7772
    • Reuter, C.J.1    Kaczowka, S.J.2    Maupin-Furlow, J.A.3
  • 27
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban, E. U., B. G. Reid, A. D. Miranker, and A. L. Horwich. 1999. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401:90-93.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 28
    • 0035043572 scopus 로고    scopus 로고
    • A new simvastatin (mevinolin)-resistance marker from Haloarcula hispanica and a new Haloferax volcanii strain cured of plasmid pHV2
    • Wendoloski, D., C. Ferrer, and M. L. Dyall-Smith. 2001. A new simvastatin (mevinolin)-resistance marker from Haloarcula hispanica and a new Haloferax volcanii strain cured of plasmid pHV2. Microbiology 147:959-964.
    • (2001) Microbiology , vol.147 , pp. 959-964
    • Wendoloski, D.1    Ferrer, C.2    Dyall-Smith, M.L.3
  • 29
    • 0032836107 scopus 로고    scopus 로고
    • Halophilic 20S proteasomes of the archaeon Haloferax volcanii: Purification, characterization, and gene sequence analysis
    • Wilson, H. L., H. C. Aldrich, and J. A. Maupin-Furlow. 1999. Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis. J. Bacteriol. 181:5814-5824.
    • (1999) J. Bacteriol. , vol.181 , pp. 5814-5824
    • Wilson, H.L.1    Aldrich, H.C.2    Maupin-Furlow, J.A.3
  • 30
    • 0242523959 scopus 로고    scopus 로고
    • A salvage pathway for protein synthesis: TmRNA and trans-translation
    • Withey, J. H., and D. I. Friedman. 2003. A salvage pathway for protein synthesis: tmRNA and trans-translation. Annu. Rev. Microbiol. 57:101-123.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 101-123
    • Withey, J.H.1    Friedman, D.I.2
  • 31
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., O. Kanlder, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kanlder, O.2    Wheelis, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.