메뉴 건너뛰기




Volumn 23, Issue 6, 2011, Pages 2348-2361

Subunit stoichiometry, evolution, and functional implications of an asymmetric plant plastid ClpP/R protease complex in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; CYANOBACTERIA; PROKARYOTA;

EID: 79960884954     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.111.086454     Document Type: Article
Times cited : (61)

References (54)
  • 1
    • 67649413592 scopus 로고    scopus 로고
    • Structure and function of a novel type of ATP-dependent Clp protease
    • Andersson, F.I., et al. (2009). Structure and function of a novel type of ATP-dependent Clp protease. J. Biol. Chem. 284: 13519-13532.
    • (2009) J. Biol. Chem , vol.284 , pp. 13519-13532
    • Andersson, F.I.1
  • 2
    • 33751228400 scopus 로고    scopus 로고
    • ATP-dependent proteases of bacteria: Recognition logic and operating principles
    • Baker, T.A., and Sauer, R.T. (2006). ATP-dependent proteases of bacteria: Recognition logic and operating principles. Trends Biochem. Sci. 31: 647-653.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 647-653
    • Baker, T.A.1    Sauer, R.T.2
  • 3
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon, R.J., Doherty, M.K., Pratt, J.M., and Gaskell, S.J. (2005). Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat. Methods 2: 587-589.
    • (2005) Nat. Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 4
    • 67649511917 scopus 로고    scopus 로고
    • Isotope dilution strategies for absolute quantitative proteomics
    • Brun, V., Masselon, C., Garin, J., and Dupuis, A. (2009). Isotope dilution strategies for absolute quantitative proteomics. J. Proteomics 72: 740-749.
    • (2009) J. Proteomics , vol.72 , pp. 740-749
    • Brun, V.1    Masselon, C.2    Garin, J.3    Dupuis, A.4
  • 7
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: A maximum likelihood approach
    • Felsenstein, J. (1981). Evolutionary trees from DNA sequences: A maximum likelihood approach. J. Mol. Evol. 17: 368-376.
    • (1981) J. Mol. Evol , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 8
    • 59849093889 scopus 로고    scopus 로고
    • Prediction of high-responding peptides for targeted protein assays by mass spectrometry
    • Fusaro, V.A., Mani, D.R., Mesirov, J.P., and Carr, S.A. (2009). Prediction of high-responding peptides for targeted protein assays by mass spectrometry. Nat. Biotechnol. 27: 190-198.
    • (2009) Nat. Biotechnol , vol.27 , pp. 190-198
    • Fusaro, V.A.1    Mani, D.R.2    Mesirov, J.P.3    Carr, S.A.4
  • 9
    • 18144426344 scopus 로고    scopus 로고
    • The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation
    • Gribun, A., Kimber, M.S., Ching, R., Sprangers, R., Fiebig, K.M., and Houry, W.A. (2005). The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 280: 16185-16196.
    • (2005) J. Biol. Chem , vol.280 , pp. 16185-16196
    • Gribun, A.1    Kimber, M.S.2    Ching, R.3    Sprangers, R.4    Fiebig, K.M.5    Houry, W.A.6
  • 11
    • 0035039711 scopus 로고    scopus 로고
    • Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease
    • Halperin, T., Zheng, B., Itzhaki, H., Clarke, A.K., and Adam, Z. (2001). Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease. Plant Mol. Biol. 45: 461-468.
    • (2001) Plant Mol. Biol , vol.45 , pp. 461-468
    • Halperin, T.1    Zheng, B.2    Itzhaki, H.3    Clarke, A.K.4    Adam, Z.5
  • 12
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck, A.J. (2008). Native mass spectrometry: A bridge between interactomics and structural biology. Nat. Methods 5: 927-933.
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.1
  • 13
    • 77955345941 scopus 로고    scopus 로고
    • Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry
    • Kaake, R.M., Wang, X., and Huang, L. (2010). Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry. Mol. Cell. Proteomics 9: 1650-1665.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1650-1665
    • Kaake, R.M.1    Wang, X.2    Huang, L.3
  • 14
    • 77957966789 scopus 로고    scopus 로고
    • New insights into the types and function of proteases in plastids
    • Kato, Y., and Sakamoto, W. (2010). New insights into the types and function of proteases in plastids. Int Rev Cell Mol Biol 280: 185-218.
    • (2010) Int Rev Cell Mol Biol , vol.280 , pp. 185-218
    • Kato, Y.1    Sakamoto, W.2
  • 15
    • 70349238699 scopus 로고    scopus 로고
    • Subunits of the plastid ClpPR protease complex have differential contributions to embryogenesis, plastid biogenesis, and plant development in Arabidopsis
    • Kim, J., Rudella, A., Ramirez Rodriguez, V., Zybailov, B., Olinares, P.D., and van Wijk, K.J. (2009). Subunits of the plastid ClpPR protease complex have differential contributions to embryogenesis, plastid biogenesis, and plant development in Arabidopsis. Plant Cell 21: 1669-1692.
    • (2009) Plant Cell , vol.21 , pp. 1669-1692
    • Kim, J.1    Rudella, A.2    Ramirez Rodriguez, V.3    Zybailov, B.4    Olinares, P.D.5    van Wijk, K.J.6
  • 16
    • 33847416604 scopus 로고    scopus 로고
    • A synthetic protein approach toward accurate mass spectrometric quantification of component stoichiometry of multiprotein complexes
    • Kito, K., Ota, K., Fujita, T., and Ito, T. (2007). A synthetic protein approach toward accurate mass spectrometric quantification of component stoichiometry of multiprotein complexes. J. Proteome Res. 6: 792-800.
    • (2007) J. Proteome Res , vol.6 , pp. 792-800
    • Kito, K.1    Ota, K.2    Fujita, T.3    Ito, T.4
  • 18
    • 33748788003 scopus 로고    scopus 로고
    • Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis
    • Krokhin, O.V., Antonovici, M., Ens, W., Wilkins, J.A., and Standing, K.G. (2006). Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis. Anal. Chem. 78: 6645-6650.
    • (2006) Anal. Chem , vol.78 , pp. 6645-6650
    • Krokhin, O.V.1    Antonovici, M.2    Ens, W.3    Wilkins, J.A.4    Standing, K.G.5
  • 20
    • 64049095981 scopus 로고    scopus 로고
    • Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry
    • Maglica, Z., Kolygo, K., and Weber-Ban, E. (2009). Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. Structure 17: 508-516.
    • (2009) Structure , vol.17 , pp. 508-516
    • Maglica, Z.1    Kolygo, K.2    Weber-Ban, E.3
  • 21
    • 27644450421 scopus 로고    scopus 로고
    • The chloroplast ClpP complex in Chlamydomonas reinhardtii contains an unusual high molecular mass subunit with a large apical domain
    • Majeran, W., Friso, G., van Wijk, K.J., and Vallon, O. (2005). The chloroplast ClpP complex in Chlamydomonas reinhardtii contains an unusual high molecular mass subunit with a large apical domain. FEBS J. 272: 5558-5571.
    • (2005) FEBS J , vol.272 , pp. 5558-5571
    • Majeran, W.1    Friso, G.2    van Wijk, K.J.3    Vallon, O.4
  • 22
    • 0032568504 scopus 로고    scopus 로고
    • Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP
    • Maurizi, M.R., Singh, S.K., Thompson, M.W., Kessel, M., and Ginsburg, A. (1998). Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry 37: 7778-7786.
    • (1998) Biochemistry , vol.37 , pp. 7778-7786
    • Maurizi, M.R.1    Singh, S.K.2    Thompson, M.W.3    Kessel, M.4    Ginsburg, A.5
  • 23
    • 42649091860 scopus 로고    scopus 로고
    • Comparative evaluation of current peptide production platforms used in absolute quantification in proteomics
    • Mirzaei, H., McBee, J.K., Watts, J., and Aebersold, R. (2008). Comparative evaluation of current peptide production platforms used in absolute quantification in proteomics. Mol. Cell. Proteomics 7: 813-823.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 813-823
    • Mirzaei, H.1    McBee, J.K.2    Watts, J.3    Aebersold, R.4
  • 24
    • 43249087428 scopus 로고    scopus 로고
    • MASIC: A software program for fast quantitation and flexible visualization of chromatographic profiles from detected LC-MS(/MS) features
    • Monroe, M.E., Shaw, J.L., Daly, D.S., Adkins, J.N., and Smith, R.D. (2008). MASIC: A software program for fast quantitation and flexible visualization of chromatographic profiles from detected LC-MS(/MS) features. Comput. Biol. Chem. 32: 215-217.
    • (2008) Comput. Biol. Chem , vol.32 , pp. 215-217
    • Monroe, M.E.1    Shaw, J.L.2    Daly, D.S.3    Adkins, J.N.4    Smith, R.D.5
  • 25
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D.G., and Heringa, J. (2000). T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302: 205-217.
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 26
    • 79958140971 scopus 로고
    • The Clp protease system: A central component of the chloroplast protease network
    • Olinares, P.D., Kim, J., and van Wijk, K.J. (2011). The Clp protease system: A central component of the chloroplast protease network. Biochim. Biophys. Acta 1807: 999-1011.
    • (1807) Biochim. Biophys. Acta , pp. 999-1011
    • Olinares, P.D.1    Kim, J.2    van Wijk, K.J.3
  • 27
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants: Their predicted three-dimensional structures, and functional implications
    • Peltier, J.B., Ripoll, D.R., Friso, G., Rudella, A., Cai, Y., Ytterberg, J., Giacomelli, L., Pillardy, J., and van Wijk, K.J. (2004). Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants: Their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 279: 4768-4781.
    • (2004) J. Biol. Chem , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, J.8    van Wijk, K.J.9
  • 28
    • 0035844248 scopus 로고    scopus 로고
    • Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana
    • Peltier, J.B., Ytterberg, J., Liberles, D.A., Roepstorff, P., and van Wijk, K.J. (2001). Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana. J. Biol. Chem. 276: 16318-16327.
    • (2001) J. Biol. Chem , vol.276 , pp. 16318-16327
    • Peltier, J.B.1    Ytterberg, J.2    Liberles, D.A.3    Roepstorff, P.4    van Wijk, K.J.5
  • 29
    • 77953911347 scopus 로고    scopus 로고
    • Mass spectrometric identification of oxidative modifications of tryp-tophan residues in proteins: Chemical artifact or post-translational modification
    • Perdivara, I., Deterding, L.J., Przybylski, M., and Tomer, K.B. (2010). Mass spectrometric identification of oxidative modifications of tryp-tophan residues in proteins: Chemical artifact or post-translational modification? J. Am. Soc. Mass Spectrom. 21: 1114-1117.
    • (2010) J. Am. Soc. Mass Spectrom , vol.21 , pp. 1114-1117
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 30
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes
    • Pratt, J.M., Simpson, D.M., Doherty, M.K., Rivers, J., Gaskell, S.J., and Beynon, R.J. (2006). Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes. Nat. Protoc. 1: 1029-1043.
    • (2006) Nat. Protoc , vol.1 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 31
    • 14844310253 scopus 로고    scopus 로고
    • An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation
    • Rubio, V., Shen, Y., Saijo, Y., Liu, Y., Gusmaroli, G., Dinesh-Kumar, S.P., and Deng, X.W. (2005). An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation. Plant J. 41: 767-778.
    • (2005) Plant J , vol.41 , pp. 767-778
    • Rubio, V.1    Shen, Y.2    Saijo, Y.3    Liu, Y.4    Gusmaroli, G.5    Dinesh-Kumar, S.P.6    Deng, X.W.7
  • 32
    • 33745782714 scopus 로고    scopus 로고
    • Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis
    • Rudella, A., Friso, G., Alonso, J.M., Ecker, J.R., and van Wijk, K.J. (2006). Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis. Plant Cell 18: 1704-1721.
    • (2006) Plant Cell , vol.18 , pp. 1704-1721
    • Rudella, A.1    Friso, G.2    Alonso, J.M.3    Ecker, J.R.4    van Wijk, K.J.5
  • 33
    • 0036068418 scopus 로고    scopus 로고
    • The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus
    • Schelin, J., Lindmark, F., and Clarke, A.K. (2002). The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus. Microbiology 148: 2255-2265.
    • (2002) Microbiology , vol.148 , pp. 2255-2265
    • Schelin, J.1    Lindmark, F.2    Clarke, A.K.3
  • 34
    • 77950395166 scopus 로고    scopus 로고
    • Determination of protein stoichiometry within protein complexes using absolute quantification and multiple reaction monitoring
    • Schmidt, C., Lenz, C., Grote, M., Löhrmann, R., and Urlaub, H. (2010). Determination of protein stoichiometry within protein complexes using absolute quantification and multiple reaction monitoring. Anal. Chem. 82: 2784-2796.
    • (2010) Anal. Chem , vol.82 , pp. 2784-2796
    • Schmidt, C.1    Lenz, C.2    Grote, M.3    Löhrmann, R.4    Urlaub, H.5
  • 35
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt, T.G., and Skerra, A. (2007). The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2: 1528-1535.
    • (2007) Nat. Protoc , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 36
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon, M., and Robinson, C.V. (2007). The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 76: 167-193.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 37
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 38
    • 79952289354 scopus 로고    scopus 로고
    • Assembly of the chloroplast ATP-dependent Clp protease in Arabidopsis is regulated by the ClpT accessory proteins
    • Sjögren, L.L., and Clarke, A.K. (2011). Assembly of the chloroplast ATP-dependent Clp protease in Arabidopsis is regulated by the ClpT accessory proteins. Plant Cell 23: 322-332.
    • (2011) Plant Cell , vol.23 , pp. 322-332
    • Sjögren, L.L.1    Clarke, A.K.2
  • 39
    • 33750969370 scopus 로고    scopus 로고
    • Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis
    • Sjögren, L.L., Stanne, T.M., Zheng, B., Sutinen, S., and Clarke, A.K. (2006). Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis. Plant Cell 18: 2635-2649.
    • (2006) Plant Cell , vol.18 , pp. 2635-2649
    • Sjögren, L.L.1    Stanne, T.M.2    Zheng, B.3    Sutinen, S.4    Clarke, A.K.5
  • 40
    • 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
  • 41
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis, A. (2006). RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22: 2688-2690.
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 42
    • 34347232349 scopus 로고    scopus 로고
    • Distinctive types of ATP-dependent Clp proteases in cyanobacteria
    • Stanne, T.M., Pojidaeva, E., Andersson, F.I., and Clarke, A.K. (2007). Distinctive types of ATP-dependent Clp proteases in cyanobacteria. J. Biol. Chem. 282: 14394-14402.
    • (2007) J. Biol. Chem , vol.282 , pp. 14394-14402
    • Stanne, T.M.1    Pojidaeva, E.2    Andersson, F.I.3    Clarke, A.K.4
  • 43
    • 64549106859 scopus 로고    scopus 로고
    • Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukary-otes
    • Striebel, F., Kress, W., and Weber-Ban, E. (2009). Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukary-otes. Curr. Opin. Struct. Biol. 19: 209-217.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 209-217
    • Striebel, F.1    Kress, W.2    Weber-Ban, E.3
  • 45
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007). MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596-1599.
    • (2007) Mol. Biol. Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 46
    • 0002671410 scopus 로고
    • Some probabilistic and statistical problems on the analysis of DNA sequences
    • R.M. Miura, ed (Providence, RI: American Mathematical Society
    • Tavar, S. (1986). Some probabilistic and statistical problems on the analysis of DNA sequences. In Some Mathematical Questions in Biology: DNA Sequence Analysis, R.M. Miura, ed (Providence, RI: American Mathematical Society), pp. 57-86.
    • (1986) Some Mathematical Questions In Biology: DNA Sequence Analysis , pp. 57-86
    • Tavar, S.1
  • 47
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
    • Wang, J., Hartling, J.A., and Flanagan, J.M. (1997). The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91: 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 48
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M., and Barton, G.J. (2009). Jalview Version 2: A multiple sequence alignment editor and analysis workbench. Bioinformatics 25: 1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 49
    • 0030451420 scopus 로고    scopus 로고
    • Among-site rate variation and its impact on phyloge-netic analyses
    • Yang, Z. (1996). Among-site rate variation and its impact on phyloge-netic analyses. Trends Ecol. Evol. (Amst.) 11: 367-372.
    • (1996) Trends Ecol. Evol. (Amst.) , vol.11 , pp. 367-372
    • Yang, Z.1
  • 50
    • 34447511284 scopus 로고    scopus 로고
    • ClpP: A distinctive family of cylindrical energy-dependent serine proteases
    • Yu, A.Y., and Houry, W.A. (2007). ClpP: A distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 581: 3749-3757.
    • (2007) FEBS Lett , vol.581 , pp. 3749-3757
    • Yu, A.Y.1    Houry, W.A.2
  • 51
    • 33845435000 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method
    • Zhang, X., Henriques, R., Lin, S.S., Niu, Q.W., and Chua, N.H. (2006). Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method. Nat. Protoc. 1: 641-646.
    • (2006) Nat. Protoc , vol.1 , pp. 641-646
    • Zhang, X.1    Henriques, R.2    Lin, S.S.3    Niu, Q.W.4    Chua, N.H.5
  • 52
    • 33748933906 scopus 로고    scopus 로고
    • A nuclear-encoded ClpP subunit of the chloroplast ATP-dependent Clp protease is essential for early development in Arabi-dopsis thaliana
    • Zheng, B., MacDonald, T.M., Sutinen, S., Hurry, V., and Clarke, A.K. (2006). A nuclear-encoded ClpP subunit of the chloroplast ATP-dependent Clp protease is essential for early development in Arabi-dopsis thaliana. Planta 224: 1103-1115.
    • (2006) Planta , vol.224 , pp. 1103-1115
    • Zheng, B.1    Macdonald, T.M.2    Sutinen, S.3    Hurry, V.4    Clarke, A.K.5
  • 53
    • 70349246174 scopus 로고    scopus 로고
    • Large scale comparative proteomics of a chloroplast Clp protease mutant reveals folding stress, altered protein homeostasis, and feedback regulation of metabolism
    • Zybailov, B., Friso, G., Kim, J., Rudella, A., Rodriguez, V.R., Asakura, Y., Sun, Q., and van Wijk, K.J. (2009b). Large scale comparative proteomics of a chloroplast Clp protease mutant reveals folding stress, altered protein homeostasis, and feedback regulation of metabolism. Mol. Cell. Proteomics 8: 1789-1810.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1789-1810
    • Zybailov, B.1    Friso, G.2    Kim, J.3    Rudella, A.4    Rodriguez, V.R.5    Asakura, Y.6    Sun, Q.7    van Wijk, K.J.8
  • 54
    • 70349622043 scopus 로고    scopus 로고
    • Workflow for large scale detection and validation of peptide modifications by RPLC-LTQ-Orbitrap: Application to the Arabidopsis thaliana leaf proteome and an online modified peptide library
    • Zybailov, B., Sun, Q., and van Wijk, K.J. (2009a). Workflow for large scale detection and validation of peptide modifications by RPLC-LTQ-Orbitrap: Application to the Arabidopsis thaliana leaf proteome and an online modified peptide library. Anal. Chem. 81: 8015-8024.
    • (2009) Anal. Chem , vol.81 , pp. 8015-8024
    • Zybailov, B.1    Sun, Q.2    van Wijk, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.