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Volumn 9, Issue 11, 2009, Pages 3079-3089

Application of quantitative immunoprecipitation combined with knockdown and cross-linking to Chlamydomonas reveals the presence of vesicle-inducing protein in plastids 1 in a common complex with chloroplast HSP90C

Author keywords

Chloroplast chaperones; MS; Protein protein interactions; RNA interference; Stable isotope labeling with amino acids in cell culture

Indexed keywords

AMINO ACID; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90C; MEMBRANE PROTEIN; PROTOZOAL PROTEIN; STABLE ISOTOPE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VESICLE INDUCING PROTEIN IN PLASTID 1;

EID: 67649198519     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800872     Document Type: Article
Times cited : (48)

References (44)
  • 5
    • 14844293494 scopus 로고    scopus 로고
    • J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1
    • Liu, C., Willmund, F., Whitelegge, J. P., Hawat, S. et al., J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1. Mol. Biol. Cell 2005, 16, 1165-1177.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1165-1177
    • Liu, C.1    Willmund, F.2    Whitelegge, J.P.3    Hawat, S.4
  • 6
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • DOI 10.1038/nmeth972, PII NMETH972
    • Selbach, M., Mann, M., Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat. Methods 2006, 3, 981-983. (Pubitemid 44782696)
    • (2006) Nature Methods , vol.3 , Issue.12 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 7
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M., Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 2006, 7, 952-958.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 8
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E., Mann, M., A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 2006, 1, 2650-2660.
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 9
    • 31444448895 scopus 로고    scopus 로고
    • RNA silencing in Chlamydomonas: Mechanisms and tools
    • Schroda, M., RNA silencing in Chlamydomonas: mechanisms and tools. Curr. Genet. 2006, 49, 69-84.
    • (2006) Curr. Genet. , vol.49 , pp. 69-84
    • Schroda, M.1
  • 10
    • 36048942406 scopus 로고    scopus 로고
    • Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii
    • DOI 10.1002/pmic.200700407
    • Naumann, B., Busch, A., Allmer, J., Ostendorf, E. et al., Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii. Proteomics 2007, 7, 3964-3979. (Pubitemid 350100012)
    • (2007) Proteomics , vol.7 , Issue.21 , pp. 3964-3979
    • Naumann, B.1    Busch, A.2    Allmer, J.3    Ostendorf, E.4    Zeller, M.5    Kirchhoff, H.6    Hippler, M.7
  • 11
    • 20144382680 scopus 로고    scopus 로고
    • N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii
    • Naumann, B., Stauber, E. J., Busch, A., Sommer, F., Hippler, M., N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii. J. Biol. Chem. 2005, 280, 20431-20441.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20431-20441
    • Naumann, B.1    Stauber, E.J.2    Busch, A.3    Sommer, F.4    Hippler, M.5
  • 12
    • 34247185926 scopus 로고    scopus 로고
    • The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas
    • DOI 10.1111/j.1365-313X.2007.03047.x
    • Liu, C., Willmund, F., Golecki, J. R., Cacace, S. et al., The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas. Plant J. 2007, 50, 265-277. (Pubitemid 46624135)
    • (2007) Plant Journal , vol.50 , Issue.2 , pp. 265-277
    • Liu, C.1    Willmund, F.2    Golecki, J.R.3    Cacace, S.4    Hess, B.5    Markert, C.6    Schroda, M.7
  • 13
    • 33745438296 scopus 로고    scopus 로고
    • One of two Alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas
    • DOI 10.1105/tpc.105.038695
    • Gohre, V., Ossenbuhl, F., Crevecoeur, M., Eichacker, L. A., Rochaix, J. D., One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas. Plant Cell 2006, 18, 1454-1466. (Pubitemid 43956109)
    • (2006) Plant Cell , vol.18 , Issue.6 , pp. 1454-1466
    • Gohre, V.1    Ossenbuhl, F.2    Crevecoeur, M.3    Eichacker, L.A.4    Rochaix, J.-D.5
  • 15
    • 0033149821 scopus 로고    scopus 로고
    • A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition
    • Schroda, M., Vallon, O., Wollman, F. A., Beck, C. F., A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition. Plant Cell 1999, 11, 1165-1178.
    • (1999) Plant Cell , vol.11 , pp. 1165-1178
    • Schroda, M.1    Vallon, O.2    Wollman, F.A.3    Beck, C.F.4
  • 16
    • 0025117612 scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • Kindle, K. L., High-frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 1990, 87, 1228-1232.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1228-1232
    • Kindle, K.L.1
  • 17
    • 35148813020 scopus 로고    scopus 로고
    • Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas
    • DOI 10.1111/j.1365-313X.2007.03228.x
    • Schulz-Raffelt, M., Lodha, M., Schroda, M., Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas. Plant J. 2007, 52, 286-295. (Pubitemid 47537578)
    • (2007) Plant Journal , vol.52 , Issue.2 , pp. 286-295
    • Schulz-Raffelt, M.1    Lodha, M.2    Schroda, M.3
  • 18
    • 33644666048 scopus 로고    scopus 로고
    • HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii
    • DOI 10.1104/pp.105.063578
    • Willmund, F., Schroda, M., HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. Plant Physiol. 2005, 138, 2310-2322. (Pubitemid 43733572)
    • (2005) Plant Physiology , vol.138 , Issue.4 , pp. 2310-2322
    • Willmund, F.1    Schroda, M.2
  • 19
    • 0035542788 scopus 로고    scopus 로고
    • The chloroplastic GrpE homolog of Chlamydomonas: Two isoforms generated by differential splicing
    • DOI 10.1105/tpc.13.12.2823
    • Schroda, M., Vallon, O., Whitelegge, J. P., Beck, C. F., Wollman, F. A., The chloroplastic GrpE homolog of Chlamydomonas: two isoforms generated by differential splicing. Plant Cell 2001, 13, 2823-2839. (Pubitemid 34096108)
    • (2001) Plant Cell , vol.13 , Issue.12 , pp. 2823-2839
    • Schroda, M.1    Vallon, O.2    Whitelegge, J.P.3    Beck, C.F.4    Wollman, F.-A.5
  • 20
    • 0024970727 scopus 로고
    • The chloroplast ATP synthase in Chlamydomonas reinhardtii. I. Characterization of its nine constitutive subunits
    • Lemaire, C., Wollman, F. A., The chloroplast ATP synthase in Chlamydomonas reinhardtii. I. Characterization of its nine constitutive subunits. J. Biol. Chem. 1989, 264, 10228-10234.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10228-10234
    • Lemaire, C.1    Wollman, F.A.2
  • 21
    • 0141585549 scopus 로고    scopus 로고
    • PRISM, a generic large scale proteomic investigation strategy for mammals
    • Kislinger, T., Rahman, K., Radulovic, D., Cox, B. et al., PRISM, a generic large scale proteomic investigation strategy for mammals. Mol. Cell Proteomics 2003, 2, 96-106.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 96-106
    • Kislinger, T.1    Rahman, K.2    Radulovic, D.3    Cox, B.4
  • 22
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R., III, Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 23
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., Yates, J. R., III, An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73, 5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 25
    • 34247874791 scopus 로고    scopus 로고
    • EST assembly supported by a draft genome sequence: An analysis of the Chlamydomonas reinhardtii transcriptome
    • DOI 10.1093/nar/gkm081
    • Jain, M., Shrager, J., Harris, E. H., Halbrook, R. et al., EST assembly supported by a draft genome sequence: an analysis of the Chlamydomonas reinhardtii transcriptome. Nucleic Acids Res. 2007, 35, 2074-2083. (Pubitemid 47061672)
    • (2007) Nucleic Acids Research , vol.35 , Issue.6 , pp. 2074-2083
    • Jain, M.1    Shrager, J.2    Harris, E.H.3    Halbrook, R.4    Grossman, A.R.5    Hauser, C.6    Vallon, O.7
  • 26
    • 1642314524 scopus 로고    scopus 로고
    • A novel proteomic screen for peptide-protein interactions
    • Schulze, W. X., Mann, M., A novel proteomic screen for peptide-protein interactions. J. Biol. Chem. 2004, 279, 10756-10764.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10756-10764
    • Schulze, W.X.1    Mann, M.2
  • 27
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567. (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 28
    • 0035191854 scopus 로고    scopus 로고
    • The abundant retinal protein of the Chlamydomonas eye is not the photoreceptor for phototaxis and photophobic responses
    • Fuhrmann, M., Stahlberg, A., Govorunova, E., Rank, S., Hegemann, P., The abundant retinal protein of the Chlamydomonas eye is not the photoreceptor for phototaxis and photophobic responses. J. Cell Sci. 2001, 114, 3857-3863. (Pubitemid 33094700)
    • (2001) Journal of Cell Science , vol.114 , Issue.21 , pp. 3857-3863
    • Fuhrmann, M.1    Stahlberg, A.2    Govorunova, E.3    Rank, S.4    Hegemann, P.5
  • 29
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • DOI 10.1046/j.1365-313X.2000.00652.x
    • Schroda, M., Blocker, D., Beck, C. F., The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J. 2000, 21, 121-131. (Pubitemid 30121306)
    • (2000) Plant Journal , vol.21 , Issue.2 , pp. 121-131
    • Schroda, M.1    Blocker, D.2    Beck, C.F.3
  • 30
    • 33947222954 scopus 로고    scopus 로고
    • Vipp1 is required for basic thylakoid membrane formation but not for the assembly of thylakoid protein complexes
    • Aseeva, E., Ossenbuhl, F., Sippel, C., Cho, W. K. et al., Vipp1 is required for basic thylakoid membrane formation but not for the assembly of thylakoid protein complexes. Plant Physiol. Biochem. 2007, 45, 119-128.
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 119-128
    • Aseeva, E.1    Ossenbuhl, F.2    Sippel, C.3    Cho, W.K.4
  • 31
    • 0035957404 scopus 로고    scopus 로고
    • VIPP1, a nuclear gene of Arabidopsis thaliana essential for thylakoid membrane formation
    • Kroll, D., Meierhoff, K., Bechtold, N., Kinoshita, M. et al., VIPP1, a nuclear gene of Arabidopsis thaliana essential for thylakoid membrane formation. Proc. Natl. Acad. Sci. USA 2001, 98, 4238-4242.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4238-4242
    • Kroll, D.1    Meierhoff, K.2    Bechtold, N.3    Kinoshita, M.4
  • 32
    • 57749111847 scopus 로고    scopus 로고
    • The chloroplast DnaJ homolog CDJ1 of Chlamydomonas reinhardtii is part of a multi-chaperone complex containing HSP70B, CGE1, and HSP90C
    • Willmund, F., Dorn, K., Schulz-Raffelt, M., Schroda, M., The chloroplast DnaJ homolog CDJ1 of Chlamydomonas reinhardtii is part of a multi-chaperone complex containing HSP70B, CGE1, and HSP90C. Plant Physiol. 2008, 148, 2070-2082.
    • (2008) Plant Physiol. , vol.148 , pp. 2070-2082
    • Willmund, F.1    Dorn, K.2    Schulz-Raffelt, M.3    Schroda, M.4
  • 33
    • 47749129274 scopus 로고    scopus 로고
    • Assistance for a chaperone: Chlamydomonas HEP2 activates plastidic HSP70B for cochaperone binding
    • Willmund, F., Hinnenberger, M., Nick, S., Schulz-Raffelt, M. et al., Assistance for a chaperone: Chlamydomonas HEP2 activates plastidic HSP70B for cochaperone binding. J. Biol. Chem. 2008, 283, 16363-16373.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16363-16373
    • Willmund, F.1    Hinnenberger, M.2    Nick, S.3    Schulz-Raffelt, M.4
  • 34
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier, L., Usherwood, Y. K., Chung, K. T., Hendershot, L.M., A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 2002, 13, 4456-4469.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 35
    • 11144249887 scopus 로고    scopus 로고
    • ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
    • Shen, Y., Hendershot, L. M., ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol. Biol. Cell 2005, 16, 40-50.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 40-50
    • Shen, Y.1    Hendershot, L.M.2
  • 37
    • 0012351964 scopus 로고    scopus 로고
    • 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC)
    • 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC). J. Proteome Res. 2003, 2, 173-181.
    • (2003) J. Proteome Res. , vol.2 , pp. 173-181
    • Ong, S.E.1    Kratchmarova, I.2    Mann, M.3
  • 38
    • 34548356772 scopus 로고    scopus 로고
    • An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics [1]
    • DOI 10.1038/nmeth0907-677, PII NMETH0907-677
    • Van Hoof, D., Pinkse, M. W., Oostwaard, D. W., Mummery, C. L. et al., An experimental correction for arginine-toproline conversion artifacts in SILAC-based quantitative proteomics. Nat. Methods 2007, 4, 677-678. (Pubitemid 47338150)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 677-678
    • Van Hoof, D.1    Pinkse, M.W.H.2    Oostwaard, D.W.-V.3    Mummery, C.L.4    Heck, A.J.R.5    Krijgsveld, J.6
  • 39
    • 11144314848 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals its secrets: Chaperone genes and the potential roles of their gene products in the chloroplast
    • Schroda, M., The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast. Photosynth. Res. 2004, 82, 221-240.
    • (2004) Photosynth. Res. , vol.82 , pp. 221-240
    • Schroda, M.1
  • 40
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L. F., Chow, Y. H., Hutchison, K. A., Perdew, G. H. et al., Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 1993, 268, 21711-21716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4
  • 41
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., Mann, M., Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 2005, 1, 252-262.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 42
    • 0030904362 scopus 로고    scopus 로고
    • A chlorate-resistant mutant defective in the regulation of nitrate reductase gene expression in arabidopsis defines a new HY locus
    • DOI 10.1105/tpc.9.1.21
    • Lin, Y., Cheng, C. L., A chlorate-resistant mutant defective in the regulation of nitrate reductase gene expression in Arabidopsis defines a new HY locus. Plant Cell 1997, 9, 21-35. (Pubitemid 27144452)
    • (1997) Plant Cell , vol.9 , Issue.1 , pp. 21-35
    • Lin, Y.1    Cheng, C.-L.2
  • 43
    • 0346034697 scopus 로고    scopus 로고
    • The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90
    • DOI 10.1046/j.1365-313X.2003.016011.x
    • Cao, D., Froehlich, J. E., Zhang, H., Cheng, C. L., The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90. Plant J. 2003, 33, 107-118. (Pubitemid 36117293)
    • (2003) Plant Journal , vol.33 , Issue.1 , pp. 107-118
    • Cao, D.1    Froehlich, J.E.2    Zhang, H.3    Cheng, C.-L.4
  • 44
    • 4143107121 scopus 로고    scopus 로고
    • Complex formation of Vipp1 depends on its alpha-helical PspA-like domain
    • Aseeva, E., Ossenbuhl, F., Eichacker, L. A., Wanner, G. et al., Complex formation of Vipp1 depends on its alpha-helical PspA-like domain. J. Biol. Chem. 2004, 279, 35535-35541.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35535-35541
    • Aseeva, E.1    Ossenbuhl, F.2    Eichacker, L.A.3    Wanner, G.4


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