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Volumn 48, Issue 1, 2006, Pages 73-84

FtsH11 protease plays a critical role in Arabidopsis thermotolerance

Author keywords

atts244 mutants; FtsH11 protease; Thermotolerance

Indexed keywords

ARABIDOPSIS THALIANA THERMO-SENSITIVE MUTANTS (ATTS) MUTANTS; FTSH11 PROTEASE; THERMOTOLERANCE;

EID: 33748632913     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2006.02855.x     Document Type: Article
Times cited : (106)

References (53)
  • 2
    • 0035083210 scopus 로고    scopus 로고
    • Unusual tolerance to high temperatures in a new herbicide-resistant D1 mutant from Glycine max (L.) Merr. cell cultures deficient in fatty acid desaturation
    • Alfonso, M., Yruela, I., Almarcegui, S., Torrado, E., Perez, M.A. and Picorel, R. (2001) Unusual tolerance to high temperatures in a new herbicide-resistant D1 mutant from Glycine max (L.) Merr. cell cultures deficient in fatty acid desaturation. Planta, 212, 573-582.
    • (2001) Planta , vol.212 , pp. 573-582
    • Alfonso, M.1    Yruela, I.2    Almarcegui, S.3    Torrado, E.4    Perez, M.A.5    Picorel, R.6
  • 3
    • 0037127195 scopus 로고    scopus 로고
    • A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo
    • Bailey, S., Thompson, E., Nixon, P.J., Horton, P., Mullineaux, C.W., Robinson, C. and Mann, N.H. (2002) A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo. J. Biol. Chem. 277, 2006-2011.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2006-2011
    • Bailey, S.1    Thompson, E.2    Nixon, P.J.3    Horton, P.4    Mullineaux, C.W.5    Robinson, C.6    Mann, N.H.7
  • 5
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R.S., Viitanen, P.V. and Vierling, E. (1996) Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32, 191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 6
    • 0020458787 scopus 로고
    • Plant productivity and environment
    • Boyer, J.S. (1982) Plant productivity and environment. Science, 218, 443-448.
    • (1982) Science , vol.218 , pp. 443-448
    • Boyer, J.S.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0034088275 scopus 로고    scopus 로고
    • Isolation of Arabidopsis mutants lacking components of acquired thermotolerance
    • Burke, J.J., O'Mahony, P.J. and Oliver, M.J. (2000) Isolation of Arabidopsis mutants lacking components of acquired thermotolerance. Plant Physiol. 123, 575-588.
    • (2000) Plant Physiol. , vol.123 , pp. 575-588
    • Burke, J.J.1    O'Mahony, P.J.2    Oliver, M.J.3
  • 9
    • 0034047936 scopus 로고    scopus 로고
    • Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease
    • Chen, M., Choi, Y., Voytas, D.F. and Rodermel, S. (2000) Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease. Plant J. 22, 303-313.
    • (2000) Plant J. , vol.22 , pp. 303-313
    • Chen, M.1    Choi, Y.2    Voytas, D.F.3    Rodermel, S.4
  • 10
    • 33744950352 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis thermosensitive mutant atts02 reveals an important role for galactolipids in thermotolerance
    • Chen, J., Burke, J.J., Xin, Z., Xu, C. and Velten, J. (2006) Characterization of the Arabidopsis thermosensitive mutant atts02 reveals an important role for galactolipids in thermotolerance. Plant Cell Environ. 29, 1437-1448.
    • (2006) Plant Cell Environ. , vol.29 , pp. 1437-1448
    • Chen, J.1    Burke, J.J.2    Xin, Z.3    Xu, C.4    Velten, J.5
  • 11
    • 0029074510 scopus 로고
    • The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
    • Deuerling, E., Paeslack, B. and Schumann, W. (1995) The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift. J. Bacteriol. 177, 4105-4112.
    • (1995) J. Bacteriol. , vol.177 , pp. 4105-4112
    • Deuerling, E.1    Paeslack, B.2    Schumann, W.3
  • 12
    • 0028821695 scopus 로고
    • The recA gene of Lactococcus lactis: Characterization and involvement in oxidative and thermal stress
    • Duwat, P., Ehrlich, S.D. and Gruss, A. (1995) The recA gene of Lactococcus lactis: characterization and involvement in oxidative and thermal stress. Mol. Microbiol. 17, 1121-1131.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1121-1131
    • Duwat, P.1    Ehrlich, S.D.2    Gruss, A.3
  • 13
    • 5444264352 scopus 로고    scopus 로고
    • Regulation of membrane fatty acid composition by temperature in mutants of Arabidopsis with alterations in membrane lipid composition
    • Falcone, D.L., Ogas, J.P. and Somerville, C.R. (2004) Regulation of membrane fatty acid composition by temperature in mutants of Arabidopsis with alterations in membrane lipid composition. BMC Plant Biol. 4, 17.
    • (2004) BMC Plant Biol. , vol.4 , pp. 17
    • Falcone, D.L.1    Ogas, J.P.2    Somerville, C.R.3
  • 14
    • 0002724395 scopus 로고
    • T-DNA insertion mutagenesis in Arabidopsis: Mutational spectrum
    • Feldmann, K.A. (1991) T-DNA insertion mutagenesis in Arabidopsis: mutational spectrum. Plant J. 1, 71-82.
    • (1991) Plant J. , vol.1 , pp. 71-82
    • Feldmann, K.A.1
  • 15
    • 0036225047 scopus 로고    scopus 로고
    • The FtsH protease is involved in development, stress response and heat shock control in Caulobacter crescentus
    • Fischer, B., Rummel, G., Aldridge, P. and Jenal, U. (2002) The FtsH protease is involved in development, stress response and heat shock control in Caulobacter crescentus. Mol. Microbiol. 44, 461-478.
    • (2002) Mol. Microbiol. , vol.44 , pp. 461-478
    • Fischer, B.1    Rummel, G.2    Aldridge, P.3    Jenal, U.4
  • 16
    • 0000808705 scopus 로고    scopus 로고
    • Production of high temperature tolerance transgenic plants through manipulation of membrane lipids
    • Gorver, A., Agarwal, M., Katiyar-Argarwal, S., Sahi, C. and Argarwal, S. (2000) Production of high temperature tolerance transgenic plants through manipulation of membrane lipids. Curr. Sci. 79, 5.
    • (2000) Curr. Sci. , vol.79 , pp. 5
    • Gorver, A.1    Agarwal, M.2    Katiyar-Argarwal, S.3    Sahi, C.4    Argarwal, S.5
  • 17
    • 0034021527 scopus 로고    scopus 로고
    • HSP101: A key component for the acquisition of thermotolerance in plants
    • Gurley, W.B. (2000) HSP101: a key component for the acquisition of thermotolerance in plants. Plant Cell, 12, 457-460.
    • (2000) Plant Cell , vol.12 , pp. 457-460
    • Gurley, W.B.1
  • 18
    • 0028985616 scopus 로고
    • Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB
    • Herman, C., Thevenet, D., D'Ari, R. and Bouloc, P. (1995) Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl Acad. Sci. USA, 92, 3516-3520.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3516-3520
    • Herman, C.1    Thevenet, D.2    D'Ari, R.3    Bouloc, P.4
  • 19
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong, S.W. and Vierling, E. (2000) Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl Acad. Sci. USA, 97, 4392-4397.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 20
    • 0034666092 scopus 로고    scopus 로고
    • The mitochondrial inner membrane AAA metalloprotease family in metazoans
    • Juhola, M.K., Shah, Z.H., Grivell, L.A. and Jacobs, H.T. (2000) The mitochondrial inner membrane AAA metalloprotease family in metazoans. FEBS Lett. 481, 91-95.
    • (2000) FEBS Lett. , vol.481 , pp. 91-95
    • Juhola, M.K.1    Shah, Z.H.2    Grivell, L.A.3    Jacobs, H.T.4
  • 21
    • 0029082019 scopus 로고
    • Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: Role of heat shock proteins
    • Kampinga, H.H., Brunsting, J.F., Stege, G.J., Burgman, P.W. and Konings, A.W. (1995) Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: role of heat shock proteins. Exp. Cell Res. 219, 536-546.
    • (1995) Exp. Cell Res. , vol.219 , pp. 536-546
    • Kampinga, H.H.1    Brunsting, J.F.2    Stege, G.J.3    Burgman, P.W.4    Konings, A.W.5
  • 23
    • 17144384471 scopus 로고    scopus 로고
    • Temperature dependence of photosynthesis in Arabidopsis plants with modifications in Rubisco activase and membrane fluidity
    • Kim, K. and Portis, A.R., Jr (2005) Temperature dependence of photosynthesis in Arabidopsis plants with modifications in Rubisco activase and membrane fluidity. Plant Cell Physiol. 46, 522-530.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 522-530
    • Kim, K.1    Portis Jr., A.R.2
  • 24
    • 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
  • 25
    • 0034194179 scopus 로고    scopus 로고
    • AAA proteases: Cellular machines for degrading membrane proteins
    • Langer, T. (2000) AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem. Sci. 25, 247-251.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 247-251
    • Langer, T.1
  • 26
    • 2342510197 scopus 로고    scopus 로고
    • Thermotolerance and antioxidant systems in Agrostis stolonifera: Involvement of salicylic acid, abscisic acid, calcium, hydrogen peroxide, and ethylene
    • Larkindale, J. and Huang, B. (2004) Thermotolerance and antioxidant systems in Agrostis stolonifera: involvement of salicylic acid, abscisic acid, calcium, hydrogen peroxide, and ethylene. J. Plant Physiol. 161, 405-413.
    • (2004) J. Plant Physiol. , vol.161 , pp. 405-413
    • Larkindale, J.1    Huang, B.2
  • 27
    • 26944443125 scopus 로고    scopus 로고
    • Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance
    • Larkindale, J., Hall, J.D., Knight, M.R. and Vierling, E. (2005) Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance. Plant Physiol. 138, 882-897.
    • (2005) Plant Physiol. , vol.138 , pp. 882-897
    • Larkindale, J.1    Hall, J.D.2    Knight, M.R.3    Vierling, E.4
  • 28
    • 0029964973 scopus 로고    scopus 로고
    • An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana
    • Lee, J.H. and Schoffl, F. (1996) An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana. Mol. Gen. Genet. 252, 11-19.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 11-19
    • Lee, J.H.1    Schoffl, F.2
  • 29
    • 26844581179 scopus 로고    scopus 로고
    • Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system
    • Lee, U., Wie, C., Escobar, M., Williams, B., Hong, S.W. and Vierling, E. (2005) Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell, 17, 559-571.
    • (2005) Plant Cell , vol.17 , pp. 559-571
    • Lee, U.1    Wie, C.2    Escobar, M.3    Williams, B.4    Hong, S.W.5    Vierling, E.6
  • 30
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl, M., Spetea, C., Hundal, T., Oppenheim, A.B., Adam, Z. and Andersson, B. (2000) The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell, 12, 419-431.
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 31
    • 0034637466 scopus 로고    scopus 로고
    • Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium Synechocystis sp. PCC 6803
    • Mann, N.H., Novac, N., Mullineaux, C.W., Newman, J., Bailey, S. and Robinson, C. (2000) Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 479, 72-77.
    • (2000) FEBS Lett. , vol.479 , pp. 72-77
    • Mann, N.H.1    Novac, N.2    Mullineaux, C.W.3    Newman, J.4    Bailey, S.5    Robinson, C.6
  • 32
    • 0031153994 scopus 로고    scopus 로고
    • Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease
    • Ostersetzer, O. and Adam, Z. (1997) Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease. Plant Cell, 9, 957-965.
    • (1997) Plant Cell , vol.9 , pp. 957-965
    • Ostersetzer, O.1    Adam, Z.2
  • 33
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R.J., Thompson, W.A. and Kriedemann, P.E. (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochem. Biophys. Acta, 975, 384-394.
    • (1989) Biochem. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 34
    • 0029762950 scopus 로고    scopus 로고
    • Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon
    • Rep, M., van Dijl, J.M., Suda, K., Schatz, G., Grivell, L.A. and Suzuki, C.K. (1996) Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Science, 274, 103-106.
    • (1996) Science , vol.274 , pp. 103-106
    • Rep, M.1    Van Dijl, J.M.2    Suda, K.3    Schatz, G.4    Grivell, L.A.5    Suzuki, C.K.6
  • 35
    • 0036668462 scopus 로고    scopus 로고
    • The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles
    • Sakamoto, W., Tamura, T., Hanba-Tomita, Y. and Murata, M. (2002) The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles. Genes Cells, 7, 769-780.
    • (2002) Genes Cells , vol.7 , pp. 769-780
    • Sakamoto, W.1    Tamura, T.2    Hanba-Tomita, Y.3    Murata, M.4
  • 36
    • 0347380954 scopus 로고    scopus 로고
    • Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes
    • Sakamoto, W., Zaltsman, A., Adam, Z. and Takahashi, Y. (2003) Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes. Plant Cell, 15, 2843-2855.
    • (2003) Plant Cell , vol.15 , pp. 2843-2855
    • Sakamoto, W.1    Zaltsman, A.2    Adam, Z.3    Takahashi, Y.4
  • 37
    • 0016627718 scopus 로고
    • Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12
    • Santos, D. and De Almeida, D.F. (1975) Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12. J. Bacteriol. 124, 1502-1507.
    • (1975) J. Bacteriol. , vol.124 , pp. 1502-1507
    • Santos, D.1    De Almeida, D.F.2
  • 38
    • 0028071874 scopus 로고
    • Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex
    • Schnall, R., Mannhaupt, G., Stucka, R., Tauer, R., Ehnle, S., Schwarzlose, C., Vetter, I. and Feldmann, H. (1994) Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast, 10, 1141-1155.
    • (1994) Yeast , vol.10 , pp. 1141-1155
    • Schnall, R.1    Mannhaupt, G.2    Stucka, R.3    Tauer, R.4    Ehnle, S.5    Schwarzlose, C.6    Vetter, I.7    Feldmann, H.8
  • 39
    • 0032965905 scopus 로고    scopus 로고
    • FtsH - A single-chain charonin?
    • Schumann, W. (1999) FtsH - a single-chain charonin? FEMS Microbiol. Rev. 23, 1-11.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 1-11
    • Schumann, W.1
  • 41
    • 0036935397 scopus 로고    scopus 로고
    • The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts
    • Sokolenko, A., Pojidaeva, E., Zinchenko, V., Panichkin, V., Glaser, V.M., Herrmann, R.G. and Shestakov, S.V. (2002) The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts. Curr. Genet. 41, 291-310.
    • (2002) Curr. Genet. , vol.41 , pp. 291-310
    • Sokolenko, A.1    Pojidaeva, E.2    Zinchenko, V.3    Panichkin, V.4    Glaser, V.M.5    Herrmann, R.G.6    Shestakov, S.V.7
  • 43
    • 0027304446 scopus 로고
    • Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae
    • Thorsness, P.E., White, K.H. and Fox, T.D. (1993) Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5418-5426.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5418-5426
    • Thorsness, P.E.1    White, K.H.2    Fox, T.D.3
  • 44
    • 0027535381 scopus 로고
    • The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression
    • Tomoyasu, T., Yuki, T., Morimura, S., Mori, H., Yamanaka, K., Niki, H., Hiraga, S. and Ogura, T. (1993) The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J. Bacteriol. 175, 1344-1351.
    • (1993) J. Bacteriol. , vol.175 , pp. 1344-1351
    • Tomoyasu, T.1    Yuki, T.2    Morimura, S.3    Mori, H.4    Yamanaka, K.5    Niki, H.6    Hiraga, S.7    Ogura, T.8
  • 45
    • 0029060112 scopus 로고
    • Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32
    • Tomoyasu, T., Gamer, J., Bukau, B. et al. (1995) Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 14, 2551-2560.
    • (1995) EMBO J. , vol.14 , pp. 2551-2560
    • Tomoyasu, T.1    Gamer, J.2    Bukau, B.3
  • 47
    • 0000321971 scopus 로고
    • The roles of heat shock proteins in plants
    • Vierling, E. (1991) The roles of heat shock proteins in plants. Annu. Rev. Plant Biol. 42, 579-620.
    • (1991) Annu. Rev. Plant Biol. , vol.42 , pp. 579-620
    • Vierling, E.1
  • 48
    • 0030020360 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae
    • Weber, E.R., Hanekamp, T. and Thorsness, P.E. (1996) Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae. Mol. Biol. Cell, 7, 307-317.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 307-317
    • Weber, E.R.1    Hanekamp, T.2    Thorsness, P.E.3
  • 49
    • 0037386867 scopus 로고    scopus 로고
    • High-throughput DNA extraction method suitable for PCR
    • Xin, Z., Velten, J.P., Oliver, M.J. and Burke, J.J. (2003) High-throughput DNA extraction method suitable for PCR. Biotechniques, 34, 820-824, 826.
    • (2003) Biotechniques , vol.34 , pp. 820-824
    • Xin, Z.1    Velten, J.P.2    Oliver, M.J.3    Burke, J.J.4
  • 50
    • 84982005535 scopus 로고
    • Plant low-molecular-mass heat-shock proteins: Their relationship to the acquisition of thermotolerance in plants
    • Yeh, K.W., Jinn, T.L., Yeh, C.H., Chen, Y.M. and Lin, C.Y. (1994) Plant low-molecular-mass heat-shock proteins: their relationship to the acquisition of thermotolerance in plants. Biotechnol. Appl. Biochem. 19 (Pt 1), 41-49.
    • (1994) Biotechnol. Appl. Biochem. , vol.19 , Issue.1 PART , pp. 41-49
    • Yeh, K.W.1    Jinn, T.L.2    Yeh, C.H.3    Chen, Y.M.4    Lin, C.Y.5
  • 51
    • 33644684616 scopus 로고    scopus 로고
    • Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes
    • Yu, F., Park, S. and Rodermel, S.R. (2005) Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes. Plant Physiol. 138, 1957-1966.
    • (2005) Plant Physiol. , vol.138 , pp. 1957-1966
    • Yu, F.1    Park, S.2    Rodermel, S.R.3
  • 52
    • 33644874521 scopus 로고    scopus 로고
    • Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis
    • Zaltsman, A., Ori, N. and Adam, Z. (2005) Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis. Plant Cell, 17, 2782-2790.
    • (2005) Plant Cell , vol.17 , pp. 2782-2790
    • Zaltsman, A.1    Ori, N.2    Adam, Z.3
  • 53
    • 26444535294 scopus 로고    scopus 로고
    • AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
    • Zelisko, A., Garcia-Lorenzo, M., Jackowski, G., Jansson, S. and Funk, C. (2005) AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence. Proc. Natl Acad. Sci. USA, 102, 13699-13704.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13699-13704
    • Zelisko, A.1    Garcia-Lorenzo, M.2    Jackowski, G.3    Jansson, S.4    Funk, C.5


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