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Volumn 180, Issue 19, 1998, Pages 5173-5182

ClpB in a cyanobacterium: Predicted structure, phylogenetic relationships, and regulation by light and temperature

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME;

EID: 0031657302     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.19.5173-5182.1998     Document Type: Article
Times cited : (24)

References (72)
  • 1
    • 0016378971 scopus 로고
    • Effect of photooxidative conditions on levels of Superoxide dismutase in Anacystis nidulans
    • Abelovich, A., D. Kellenber, and M. Shilo. 1974. Effect of photooxidative conditions on levels of Superoxide dismutase in Anacystis nidulans. Photochem. Photobiol. 19:379-382.
    • (1974) Photochem. Photobiol. , vol.19 , pp. 379-382
    • Abelovich, A.1    Kellenber, D.2    Shilo, M.3
  • 2
    • 84984087585 scopus 로고
    • Simple conditions for the growth of unicellular blue-green algae on plates
    • Allen, M. 1968. Simple conditions for the growth of unicellular blue-green algae on plates. J. Phycol. 4:1-3.
    • (1968) J. Phycol. , vol.4 , pp. 1-3
    • Allen, M.1
  • 3
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., K. Liberek, D. Skowyra, M. Zylicz, and C. Georgopolous. 1991. Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266:24233-24236.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopolous, C.5
  • 4
    • 0016861525 scopus 로고
    • Superoxide dismutase from a blue green alga, Plectonema boryanum
    • Asada, K., K. Yoshikama, M. Takahashi, Y. Maeda, and K. Enmanji. 1975. Superoxide dismutase from a blue green alga, Plectonema boryanum. J. Biol. Chem. 250:2801-2807.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2801-2807
    • Asada, K.1    Yoshikama, K.2    Takahashi, M.3    Maeda, Y.4    Enmanji, K.5
  • 6
    • 85004911383 scopus 로고
    • Positional flexibilities of amino acid residues in globular proteins
    • Bhaskaran, R., and P. K. Ponnuswamy. 1988. Positional flexibilities of amino acid residues in globular proteins. Int. J. Pept. Prot. Res. 32:241-255.
    • (1988) Int. J. Pept. Prot. Res. , vol.32 , pp. 241-255
    • Bhaskaran, R.1    Ponnuswamy, P.K.2
  • 7
    • 1642514170 scopus 로고
    • Biosynthesis of chloroplast carotenoids
    • M. Balscheffsky (ed.), Kluwer Academic Publishers, Dorderecht, The Netherlands
    • Britten, G. 1990. Biosynthesis of chloroplast carotenoids, p. 827-834. In M. Balscheffsky (ed.), Current research in photosynthesis, vol. 4. Kluwer Academic Publishers, Dorderecht, The Netherlands.
    • (1990) Current Research in Photosynthesis , vol.4 , pp. 827-834
    • Britten, G.1
  • 8
    • 0028872248 scopus 로고
    • Characterization of four Superoxide dismutase genes from a filamentous cyanobacterium
    • Campbell, W. S., and D. E. Laudenbach. 1994. Characterization of four Superoxide dismutase genes from a filamentous cyanobacterium. J. Bacteriol. 177:964-972.
    • (1994) J. Bacteriol. , vol.177 , pp. 964-972
    • Campbell, W.S.1    Laudenbach, D.E.2
  • 9
  • 11
    • 0000523021 scopus 로고
    • Carotenoids
    • T. W. Goodwill (ed.), Academic Press, London, United Kingdom
    • Davies, B. H. 1976. Carotenoids, p. 38-155. In T. W. Goodwill (ed.), Chemistry and biochemistry of plant pigments, vol. 2. Academic Press, London, United Kingdom.
    • (1976) Chemistry and Biochemistry of Plant Pigments , vol.2 , pp. 38-155
    • Davies, B.H.1
  • 14
    • 0001937138 scopus 로고
    • Stress-induced accumulation of xanthophyll rhodoxanthin in leaves of Aloe vera
    • Diaz, M., E. Ball, and U. Luttge. 1990. Stress-induced accumulation of xanthophyll rhodoxanthin in leaves of Aloe vera. Plant Physiol. Biochem. 28:679-682.
    • (1990) Plant Physiol. Biochem. , vol.28 , pp. 679-682
    • Diaz, M.1    Ball, E.2    Luttge, U.3
  • 15
    • 0029785532 scopus 로고    scopus 로고
    • The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC7942
    • Erikssen, M., and A. K. Clarke. 1996. The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC7942. J. Bacteriol. 178:4839-4846.
    • (1996) J. Bacteriol. , vol.178 , pp. 4839-4846
    • Erikssen, M.1    Clarke, A.K.2
  • 16
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: Inference and reliability
    • Felsenstein, J. 1988. Phylogenies from molecular sequences: inference and reliability. Annu. Rev. Genet. 22:521-565.
    • (1988) Annu. Rev. Genet. , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 17
    • 0028268401 scopus 로고
    • Sequence similarity presenter: A tool for the graphic display of similarities of long sequences for use in presentations
    • Frohlich, K. 1994. Sequence similarity presenter: a tool for the graphic display of similarities of long sequences for use in presentations. Comput. Appl. Biosci. 10:179-183.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 179-183
    • Frohlich, K.1
  • 18
    • 0030021268 scopus 로고    scopus 로고
    • Photosystem II excitation pressure and development of resistance to photoinhibition
    • Gray, G. R., L. V. Savitch, A. G. Ivanov, and N. P. A. Huner. 1996. Photosystem II excitation pressure and development of resistance to photoinhibition. Plant Physiol. 110:61-71.
    • (1996) Plant Physiol. , vol.110 , pp. 61-71
    • Gray, G.R.1    Savitch, L.V.2    Ivanov, A.G.3    Huner, N.P.A.4
  • 21
    • 0001785421 scopus 로고
    • The reversible, light-induced conversion of xathophylls in the chloroplast
    • F. C. Czygan (ed.), Fischer Publishers, Stuttgart, Germany
    • Hager, A. 1980. The reversible, light-induced conversion of xathophylls in the chloroplast. In F. C. Czygan (ed.), Pigments in plants, p. 57-79. Fischer Publishers, Stuttgart, Germany.
    • (1980) Pigments in Plants , pp. 57-79
    • Hager, A.1
  • 22
    • 0025352896 scopus 로고
    • Mutation of phosphorylation sites in lamin A that prevents nuclear lamina dissembly in mitosis
    • Heald, R., and F. McKeon. 1990. Mutation of phosphorylation sites in lamin A that prevents nuclear lamina dissembly in mitosis. Cell 61:579-589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 23
    • 0028958754 scopus 로고
    • A member of the Clp family of stress proteins is expressed during heat shock in Leishmania spp
    • Hübel, A., S. Brandau, A. Dresel, and J. Clos. 1995. A member of the Clp family of stress proteins is expressed during heat shock in Leishmania spp. Mol. Biochem. Parasital. 70:107-118.
    • (1995) Mol. Biochem. Parasital. , vol.70 , pp. 107-118
    • Hübel, A.1    Brandau, S.2    Dresel, A.3    Clos, J.4
  • 24
    • 0002468603 scopus 로고
    • Effects of long-term photoinhibition on growth and photosynthesis of cold hardened spring and winter wheat
    • Hurry, V. M., M. Krol, G. Oquist, and N. P. A. Huner. 1992. Effects of long-term photoinhibition on growth and photosynthesis of cold hardened spring and winter wheat. Planta 188:369-375.
    • (1992) Planta , vol.188 , pp. 369-375
    • Hurry, V.M.1    Krol, M.2    Oquist, G.3    Huner, N.P.A.4
  • 25
    • 0023393591 scopus 로고
    • Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La
    • Hwang, B. J., W. J. Park, C. H. Chung, and A. L. Goldberg. 1987. Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La. Proc. Natl. Acad. Sci. USA 84:5550-5554.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5550-5554
    • Hwang, B.J.1    Park, W.J.2    Chung, C.H.3    Goldberg, A.L.4
  • 26
    • 0029153942 scopus 로고
    • Abscisic acid induced protection against photoinhibition of PSII correlates with enhanced activity of the xanthophyll cycle
    • Ivanov, A. G., M. Krol, D. P. Maxwell, and N. P. A. Huner. 1995. Abscisic acid induced protection against photoinhibition of PSII correlates with enhanced activity of the xanthophyll cycle. FEBS Lett. 371:61-64.
    • (1995) FEBS Lett. , vol.371 , pp. 61-64
    • Ivanov, A.G.1    Krol, M.2    Maxwell, D.P.3    Huner, N.P.A.4
  • 27
    • 0001396452 scopus 로고
    • New spectrophotometric equations for determining chlorophyll a, b, c1, c2 in higher plants, algae and natural phytoplankton
    • Jeffrey, S. W., and G. F. Humphrey. 1975. New spectrophotometric equations for determining chlorophyll a, b, c1, c2 in higher plants, algae and natural phytoplankton. Biochem. Physiol. Pflanz. 167:191-194.
    • (1975) Biochem. Physiol. Pflanz. , vol.167 , pp. 191-194
    • Jeffrey, S.W.1    Humphrey, G.F.2
  • 28
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones, D. T., W. R. Taylor, and J. M. Thornton. 1992. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8:275-282.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 29
    • 0023184358 scopus 로고
    • A multiple-component, ATP-dependent protease from Escherica coli
    • Katayama-Fujimara, Y., S. Grottesman, and M. R. Mauirizi. 1987. A multiple-component, ATP-dependent protease from Escherica coli. J. Biol. Chem. 262:4477-4485.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4477-4485
    • Katayama-Fujimara, Y.1    Grottesman, S.2    Mauirizi, M.R.3
  • 30
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli clpAP protease and the eukaryotic 26 S proteasome
    • Kessel, M., M. R. Maurizi, B. Kim, E. Koscis, B. L. Trus, K. Singh, and A. C. Steven. 1995. Homology in structural organization between E. coli clpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250:587-594.
    • (1995) J. Mol. Biol. , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Koscis, E.4    Trus, B.L.5    Singh, K.6    Steven, A.C.7
  • 31
    • 0025768061 scopus 로고
    • Expression of the ATP-dependent protease regulatory subunit in Escherichia coli is controlled by a heat shock sigma factor (sigma 32)
    • Kitagawa, M., C. Wada, S. Yoshioka, and T. Yura. 1991. Expression of the ATP-dependent protease regulatory subunit in Escherichia coli is controlled by a heat shock sigma factor (sigma 32). J. Bacteriol. 173:4247-4253.
    • (1991) J. Bacteriol. , vol.173 , pp. 4247-4253
    • Kitagawa, M.1    Wada, C.2    Yoshioka, S.3    Yura, T.4
  • 32
    • 0029852402 scopus 로고    scopus 로고
    • Degradation of proteases Lon, Clp, and HtrA of Escherichia coli proteins aggregated in vivo by heat shock: TtrA protease action in vivo and in vitro
    • Laskowska, E., D. Kuczynska-Wisnik, J. Skorko-Glonek, and A. Taylor. 1996. Degradation of proteases Lon, Clp, and HtrA of Escherichia coli proteins aggregated in vivo by heat shock: TtrA protease action in vivo and in vitro. Mol. Microbiol. 22:555-571.
    • (1996) Mol. Microbiol. , vol.22 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skorko-Glonek, J.3    Taylor, A.4
  • 33
    • 0023750780 scopus 로고
    • Isolation, sequence analysis, and transcriptional studies of the flavodoxin gene from Anacystis nidulans R2
    • Laudenbach, D. E., M. E. Reith, and N. A. Straus. 1988. Isolation, sequence analysis, and transcriptional studies of the flavodoxin gene from Anacystis nidulans R2. J. Bacteriol. 170:258-265.
    • (1988) J. Bacteriol. , vol.170 , pp. 258-265
    • Laudenbach, D.E.1    Reith, M.E.2    Straus, N.A.3
  • 34
    • 0028675574 scopus 로고    scopus 로고
    • A soybean 101-kD heat shock protein complements a yeast hsp104 deletion mutant in acquiring thermotolerance
    • Lee, Y. J., R. T. Nagao, and J. L. Key. 1996. A soybean 101-kD heat shock protein complements a yeast hsp104 deletion mutant in acquiring thermotolerance. Plant Cell 6:1889-1897.
    • (1996) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.J.1    Nagao, R.T.2    Key, J.L.3
  • 35
    • 0027445711 scopus 로고
    • HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases
    • Leonhardt, S. A., K. Fearon, P. N. Danese, and T. L. Mason. 1993. HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol. Cell. Biol. 13:6304-6313.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6304-6313
    • Leonhardt, S.A.1    Fearon, K.2    Danese, P.N.3    Mason, T.L.4
  • 36
    • 0026935588 scopus 로고
    • Heat-shock proteins and stress tolerance in microorganisms
    • Lindquist, S. 1992. Heat-shock proteins and stress tolerance in microorganisms. Curr. Opin. Genet. Dev. 2:748-755.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 748-755
    • Lindquist, S.1
  • 37
    • 0017185653 scopus 로고
    • Purification and physical properties of Superoxide dismulase from two photosynthetic microorganisms
    • Lumsden, J., R. Cammack, and D. O. Hall. 1976. Purification and physical properties of Superoxide dismulase from two photosynthetic microorganisms. Biochim. Biophys. Acta 438:380-392.
    • (1976) Biochim. Biophys. Acta , vol.438 , pp. 380-392
    • Lumsden, J.1    Cammack, R.2    Hall, D.O.3
  • 38
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas, A. 1996. Prediction and analysis of coiled-coil structures. Methods Enzymol. 266:513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 39
    • 0029200332 scopus 로고
    • Redox regulation of light-harvesting complex II and cab mRNA abundance in Dunaliella salina
    • Maxwell, D. P., D. E. Laudenbach, and N. P. A. Huner. 1995. Redox regulation of light-harvesting complex II and cab mRNA abundance in Dunaliella salina. Plant Physiol. 109:787-795.
    • (1995) Plant Physiol. , vol.109 , pp. 787-795
    • Maxwell, D.P.1    Laudenbach, D.E.2    Huner, N.P.A.3
  • 40
    • 0016610311 scopus 로고
    • Purification properties of Superoxide dismutase from a blue-green alga
    • Misra, H. P., and B. B. Keele. 1975. Purification properties of Superoxide dismutase from a blue-green alga. Biochim. Biophys. Acta 379:418-425.
    • (1975) Biochim. Biophys. Acta , vol.379 , pp. 418-425
    • Misra, H.P.1    Keele, B.B.2
  • 41
    • 0030462757 scopus 로고    scopus 로고
    • Isolation and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in E. coli
    • Missiakas, D., F. Schwager, J.-M. Betton, C. Georggopolous, and S. Raina. 1996. Isolation and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in E. coli. EMBO J. 15:6899-6909.
    • (1996) EMBO J. , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.-M.3    Georggopolous, C.4    Raina, S.5
  • 42
    • 77957095680 scopus 로고
    • Isolation of cyanobacterial plasma membranes
    • Murata, N., and T. Omata. 1988. Isolation of cyanobacterial plasma membranes. Methods Enzymol. 167:245-251.
    • (1988) Methods Enzymol. , vol.167 , pp. 245-251
    • Murata, N.1    Omata, T.2
  • 43
    • 0025933503 scopus 로고
    • Expert system for predicting protein localization sites in gram-negative bacteria
    • Nakai, K., and M. Kanehisa. 1991. Expert system for predicting protein localization sites in gram-negative bacteria. Proteins Struct. Funct. Genet. 11:95-110.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 44
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. B., and C. D. Wunsch. 1970. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 45
    • 0028986364 scopus 로고
    • Genes encoded on a cyanobacterial plasmid are transcriptionally regulated by sulfur availability and CysR
    • Nicholson, M. L., and D. E. Laudenbach. 1995. Genes encoded on a cyanobacterial plasmid are transcriptionally regulated by sulfur availability and CysR. J. Bacteriol. 177:2143-2150.
    • (1995) J. Bacteriol. , vol.177 , pp. 2143-2150
    • Nicholson, M.L.1    Laudenbach, D.E.2
  • 46
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosine tail
    • Offer, G. 1990. Skip residues correlate with bends in the myosine tail. J. Mol. Biol. 216:213-218.
    • (1990) J. Mol. Biol. , vol.216 , pp. 213-218
    • Offer, G.1
  • 47
    • 0000932287 scopus 로고
    • Cold hardening induced resistance to photoinhibition of photosynthesis in winter rye is dependent upon an increased capacity for photosynthesis
    • Oquist, G., and N. P. A. Huner. 1993. Cold hardening induced resistance to photoinhibition of photosynthesis in winter rye is dependent upon an increased capacity for photosynthesis. Planta 189:150-156.
    • (1993) Planta , vol.189 , pp. 150-156
    • Oquist, G.1    Huner, N.P.A.2
  • 48
    • 0025777272 scopus 로고
    • HSP104 is a highly conserved protein with two essential nucleotide-binding sites
    • Parsell, D. A., Y. Sanchez, J. D. Stitzel, and S. Lindquist. 1991. HSP104 is a highly conserved protein with two essential nucleotide-binding sites. Nature (London) 353:270-273.
    • (1991) Nature (London) , vol.353 , pp. 270-273
    • Parsell, D.A.1    Sanchez, Y.2    Stitzel, J.D.3    Lindquist, S.4
  • 49
    • 10144262711 scopus 로고
    • The role of heat-shock proteins in thermotolerance
    • R. J. Ellis, R. A. Laskey, and G. H. Lorimer (ed.). Chapman & Hall, London, United Kingdom
    • Parsell, D. A., J. Taulien, and S. Lindquist. 1993. The role of heat-shock proteins in thermotolerance. In R. J. Ellis, R. A. Laskey, and G. H. Lorimer (ed.). Molecular chaperones, p. 23-30. Chapman & Hall, London, United Kingdom.
    • (1993) Molecular Chaperones , pp. 23-30
    • Parsell, D.A.1    Taulien, J.2    Lindquist, S.3
  • 50
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation?
    • Pinna, L. A. 1990. Casein kinase 2: an 'eminence grise' in cellular regulation? Biochem. Biophys. Acta 1054:267-284.
    • (1990) Biochem. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 51
    • 0030840922 scopus 로고    scopus 로고
    • Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Porankiewicz, J., and A. K. Clarke. 1997. Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942. J. Bacteriol. 179:5111-5117.
    • (1997) J. Bacteriol. , vol.179 , pp. 5111-5117
    • Porankiewicz, J.1    Clarke, A.K.2
  • 52
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powel, S. B. 1984. Photoinhibition of photosynthesis induced by visible light. Annu. Rev. Plant Physiol. 35:15-44.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 15-44
    • Powel, S.B.1
  • 53
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 55
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez, Y., and S. L. Lindquist. 1990. HSP104 required for induced thermotolerance. Science 248:1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 56
    • 0026523626 scopus 로고
    • HSP104 is required for tolerance to many forms of stress
    • Sanchez, Y., J. Taulien, K. A. Borkovich, and S. L. Lindquist. 1992. HSP104 is required for tolerance to many forms of stress. EMBO J. 11:2357-2364.
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.L.4
  • 57
    • 0000667335 scopus 로고    scopus 로고
    • Photosystem II excitation pressure and photosynthetic carbon metabolism in Chlorella vulgaris
    • Savitch, L. V., D. P. Maxwell, and N. P. A. Huner. 1996. Photosystem II excitation pressure and photosynthetic carbon metabolism in Chlorella vulgaris. Plant Physiol. 111:127-136.
    • (1996) Plant Physiol. , vol.111 , pp. 127-136
    • Savitch, L.V.1    Maxwell, D.P.2    Huner, N.P.A.3
  • 58
    • 0030219939 scopus 로고    scopus 로고
    • The HSP100/clp proteins: A common mechanism explains diverse functions
    • Schirmer, E. C., J. R. Glover, M. A. Singer, and S. Lindquist. 1996. The HSP100/clp proteins: a common mechanism explains diverse functions. Trends Biochem. Sci. 21:289-296.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 289-296
    • Schirmer, E.C.1    Glover, J.R.2    Singer, M.A.3    Lindquist, S.4
  • 59
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin, J., N. D. DeWitt, and J. M. Flanagan. 1995. The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant Cell 7:1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 60
    • 84865558951 scopus 로고
    • The role of carotenoids in protection against photoinhibition
    • Y. P. Abrol, P. Mohanty and P. Govindjee (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Sharma, P. K., and D. O. Hall. 1991. The role of carotenoids in protection against photoinhibition. In Y. P. Abrol, P. Mohanty and P. Govindjee (ed.), Photosynthesis: photoreactions to plant productivity. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1991) Photosynthesis: Photoreactions to Plant Productivity
    • Sharma, P.K.1    Hall, D.O.2
  • 62
    • 0026571094 scopus 로고
    • The Clp proteins: Proteolysis regulators or molecular chaperones?
    • Squires, C., and C. L. Squires. 1992. The Clp proteins: proteolysis regulators or molecular chaperones? J. Bacteriol. 174:1081-1085.
    • (1992) J. Bacteriol. , vol.174 , pp. 1081-1085
    • Squires, C.1    Squires, C.L.2
  • 63
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires, C. L., S. Pedersen, B. M. Ross, and C. Squires. 1991. ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173:4254-4262.
    • (1991) J. Bacteriol. , vol.173 , pp. 4254-4262
    • Squires, C.L.1    Pedersen, S.2    Ross, B.M.3    Squires, C.4
  • 64
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer, K., and A. von Haeseler. 1996. Quartet puzzling: a quartet maximum likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13:964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 66
    • 0028013177 scopus 로고
    • Improved sensitivity of profile searches through the use of sequence weights and gap excision
    • Thompson, J. D., G. Higgins, and T. J. Gibson. 1994. Improved sensitivity of profile searches through the use of sequence weights and gap excision. Comput. Appl. Biosci. 10:19-29.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 19-29
    • Thompson, J.D.1    Higgins, G.2    Gibson, T.J.3
  • 67
    • 0001607723 scopus 로고
    • Distantly related sequences at the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Sarasti, M. S. Runswick, and N. S. Gay. 1982. Distantly related sequences at the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-950.
    • (1982) EMBO J. , vol.1 , pp. 945-950
    • Walker, J.E.1    Sarasti, M.2    Runswick, M.S.3    Gay, N.S.4
  • 68
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., D. Wojtkowiak, J. Marszalek, B. Banecki, M. Jonsen, B. Graves, C. Georgopolous, and M. Zylicz. 1995. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14:1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopolous, C.7    Zylicz, M.8
  • 70
    • 0027519423 scopus 로고
    • Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli
    • Wojtkowiak, D., C. Georgopoulos, and M. Zylicz. 1993. Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268:22609-22617.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22609-22617
    • Wojtkowiak, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 71
    • 0024552829 scopus 로고
    • Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides
    • Woo, K. M., W. J. Chung, D. B. Ha, A. L. Goldberg, and C. H. Chung. 1989. Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. J. Biol. Chem. 264:2088-2091.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2088-2091
    • Woo, K.M.1    Chung, W.J.2    Ha, D.B.3    Goldberg, A.L.4    Chung, C.H.5
  • 72
    • 0001592716 scopus 로고
    • The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase
    • Woo, K. M., K. I. Kim, A. L. Goldberg, D. B. Ha, and C. H. Chung. 1992. The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J. Biol. Chem. 267:20429-20434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20429-20434
    • Woo, K.M.1    Kim, K.I.2    Goldberg, A.L.3    Ha, D.B.4    Chung, C.H.5


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