메뉴 건너뛰기




Volumn 96, Issue 9, 2009, Pages 3620-3628

Site-directed spin-labeling study of the light-harvesting complex CP29

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; APOPROTEIN; CYSTEINE; MEMBRANE PROTEIN; NITROXIDE; PROTEIN; THREONINE; ARABIDOPSIS PROTEIN; CAROTENOID; CP29 LIGHT HARVESTING COMPLEX;

EID: 67650394201     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.01.038     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • Nelson, N., and C. F. Yocum. 2006. Structure and function of photosystems I and II. Annu. Rev. Plant Biol. 57:521-565.
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 2
    • 0033012091 scopus 로고    scopus 로고
    • A guide to the Lhc genes and their relatives in Arabidopsis
    • Jansson, S. 1999. A guide to the Lhc genes and their relatives in Arabidopsis. Trends Plant Sci. 4:236-240.
    • (1999) Trends Plant Sci , vol.4 , pp. 236-240
    • Jansson, S.1
  • 3
    • 3242665135 scopus 로고    scopus 로고
    • A look within LHCII: Differential analysis of the Lhcb1-3 complexes building the major trimeric antenna complex of higher-plant photosynthesis
    • Caffarri, S., R. Croce, L. Cattivelli, and R. Bassi. 2004. A look within LHCII: differential analysis of the Lhcb1-3 complexes building the major trimeric antenna complex of higher-plant photosynthesis. Biochemistry. 43:9467-9476.
    • (2004) Biochemistry , vol.43 , pp. 9467-9476
    • Caffarri, S.1    Croce, R.2    Cattivelli, L.3    Bassi, R.4
  • 4
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker, J. P., and E. J. Boekema. 2005. Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta. 1706:12-39.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 5
    • 41249094699 scopus 로고    scopus 로고
    • Zeaxanthin radical cation formation in minor light-harvesting complexes of higher plant antenna
    • Avenson, T. J., T. K. Ahn, D. Zigmantas, K. K. Niyogi, Z. Li, et al. 2008. Zeaxanthin radical cation formation in minor light-harvesting complexes of higher plant antenna. J. Biol. Chem. 283:3550-3558.
    • (2008) J. Biol. Chem , vol.283 , pp. 3550-3558
    • Avenson, T.J.1    Ahn, T.K.2    Zigmantas, D.3    Niyogi, K.K.4    Li, Z.5
  • 6
    • 44049086448 scopus 로고    scopus 로고
    • Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein
    • Ahn, T. K., T. J. Avenson, M. Ballottari, Y.-C. Cheng, K. K. Niyogi, et al. 2008. Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein. Science. 320:794-797.
    • (2008) Science , vol.320 , pp. 794-797
    • Ahn, T.K.1    Avenson, T.J.2    Ballottari, M.3    Cheng, Y.-C.4    Niyogi, K.K.5
  • 7
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu, Z., H. Yan, K. Wang, T. Kuang, J. Zhang, et al. 2004. Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature. 428:287-292.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5
  • 9
    • 0033621082 scopus 로고    scopus 로고
    • Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites
    • Bassi, R., R. Croce, D. Cugini, and D. Sandonà. 1999. Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites. Proc. Natl. Acad. Sci. USA. 96:10056-10061.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10056-10061
    • Bassi, R.1    Croce, R.2    Cugini, D.3    Sandonà, D.4
  • 10
    • 0032317945 scopus 로고    scopus 로고
    • Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties
    • Sandonà, D., R. Croce, A. Pagano, M. Crimi, and R. Bassi. 1998. Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties. Biochim. Biophys. Acta. 1365:207-214.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 207-214
    • Sandonà, D.1    Croce, R.2    Pagano, A.3    Crimi, M.4    Bassi, R.5
  • 11
    • 0030590883 scopus 로고    scopus 로고
    • A CK2 site is reversibly phosphorylated in the photosystem II subunit CP29
    • Testi, M. G., R. Croce, P. P.-D. Laureto, and R. Bassi. 1996. A CK2 site is reversibly phosphorylated in the photosystem II subunit CP29. FEBS Lett. 399:245-250.
    • (1996) FEBS Lett , vol.399 , pp. 245-250
    • Testi, M.G.1    Croce, R.2    Laureto, P.P.-D.3    Bassi, R.4
  • 12
    • 0029739337 scopus 로고    scopus 로고
    • Conformational changes induced by phosphorylation in the CP29 subunit of Photosystem II
    • Croce, R., J. Breton, and R. Bassi. 1996. Conformational changes induced by phosphorylation in the CP29 subunit of Photosystem II. Biochemistry. 35:11142-11148.
    • (1996) Biochemistry , vol.35 , pp. 11142-11148
    • Croce, R.1    Breton, J.2    Bassi, R.3
  • 13
    • 0031403568 scopus 로고    scopus 로고
    • Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit, CP29
    • Mauro, S., P. Dainese, R. Lannoye, and R. Bassi. 1997. Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit, CP29. Plant Physiol. 115:171-180.
    • (1997) Plant Physiol , vol.115 , pp. 171-180
    • Mauro, S.1    Dainese, P.2    Lannoye, R.3    Bassi, R.4
  • 14
    • 36348940282 scopus 로고    scopus 로고
    • Hemminga M. A, and L. J. Berliner, editors, Springer, New York
    • Hemminga M. A., and L. J. Berliner, editors. 2007. ESR spectroscopy in membrane biophysics. Springer, New York.
    • (2007) ESR spectroscopy in membrane biophysics
  • 15
    • 59649124429 scopus 로고    scopus 로고
    • Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29
    • Van Oort, B., S. Murali, E. Wientjes, R. B. M. Koehorst, R. B. Spruijt, et al. 2009. Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29. Chem. Phys. 357:113-119.
    • (2009) Chem. Phys , vol.357 , pp. 113-119
    • Van Oort, B.1    Murali, S.2    Wientjes, E.3    Koehorst, R.B.M.4    Spruijt, R.B.5
  • 16
    • 28944451650 scopus 로고    scopus 로고
    • Exploring the local conformational space of a membrane protein by site-directed spin labeling
    • Stopar, D., J. Štrancar, R. B. Spruijt, and M. A. Hemminga. 2005. Exploring the local conformational space of a membrane protein by site-directed spin labeling. J. Chem. Inf. Model. 45:1621-1627.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 1621-1627
    • Stopar, D.1    Štrancar, J.2    Spruijt, R.B.3    Hemminga, M.A.4
  • 17
    • 0023517015 scopus 로고
    • Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli
    • Nagai, K., and H. C. Thøgersen. 1987. Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli. Methods Enzymol. 153:461-481.
    • (1987) Methods Enzymol , vol.153 , pp. 461-481
    • Nagai, K.1    Thøgersen, H.C.2
  • 18
    • 0001456147 scopus 로고
    • Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed inEscherichia coli
    • Paulsen, H., U. Rümler, and W. Rüdiger. 1990. Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed inEscherichia coli. Planta. 181:204-211.
    • (1990) Planta , vol.181 , pp. 204-211
    • Paulsen, H.1    Rümler, U.2    Rüdiger, W.3
  • 19
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R. J., W. A. Thompson, and P. E. Kriedemann. 1989. Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta. 975:384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 20
    • 0000523021 scopus 로고
    • Analysis of carotenoid pigments
    • Pigments. T. W. Goodwin, editor. Academy Press, New York
    • Davies, B. 1965. Analysis of carotenoid pigments. In Chemistry and Biochemistry of Plant Pigments. T. W. Goodwin, editor. Academy Press, New York. 489-532.
    • (1965) Chemistry and Biochemistry of Plant , pp. 489-532
    • Davies, B.1
  • 21
    • 0029967212 scopus 로고    scopus 로고
    • Reconstitution and pigment-binding properties of recombinant CP29
    • Giuffra, E., D. Cugini, R. Croce, and R. Bassi. 1996. Reconstitution and pigment-binding properties of recombinant CP29. Eur. J. Biochem. 238:112-120.
    • (1996) Eur. J. Biochem , vol.238 , pp. 112-120
    • Giuffra, E.1    Cugini, D.2    Croce, R.3    Bassi, R.4
  • 22
    • 0037381881 scopus 로고    scopus 로고
    • Energy transfer pathways in the minor antenna complex CP29 of photosystem II: A femtosecond study of carotenoid to chlorophyll transfer on mutant and WT complexes
    • Croce, R., M. G. Muller, S. Caffarri, R. Bassi, and A. R. Holzwarth. 2003. Energy transfer pathways in the minor antenna complex CP29 of photosystem II: a femtosecond study of carotenoid to chlorophyll transfer on mutant and WT complexes. Biophys. J. 84:2517-2532.
    • (2003) Biophys. J , vol.84 , pp. 2517-2532
    • Croce, R.1    Muller, M.G.2    Caffarri, S.3    Bassi, R.4    Holzwarth, A.R.5
  • 23
    • 33751211866 scopus 로고    scopus 로고
    • Motional restrictions of membrane proteins: A site-directed spin labeling study
    • Stopar, D., J. Štrancar, R. B. Spruijt, and M. A. Hemminga. 2006. Motional restrictions of membrane proteins: A site-directed spin labeling study. Biophys. J. 91:3341-3348.
    • (2006) Biophys. J , vol.91 , pp. 3341-3348
    • Stopar, D.1    Štrancar, J.2    Spruijt, R.B.3    Hemminga, M.A.4
  • 24
    • 0002323257 scopus 로고    scopus 로고
    • Tuning EPR spectral parameters with a genetic algorithm
    • Filipič, B., and J. Štrancar. 2001. Tuning EPR spectral parameters with a genetic algorithm. Appl. Soft Comput. 1:83-90.
    • (2001) Appl. Soft Comput , vol.1 , pp. 83-90
    • Filipič, B.1    Štrancar, J.2
  • 26
    • 28944453533 scopus 로고    scopus 로고
    • Speeding up a genetic algorithm for EPR-based spin label characterization of biosystem complexity
    • Kavalenka, A. A., B. Filipič, M. A. Hemminga, and J. Štrancar. 2005. Speeding up a genetic algorithm for EPR-based spin label characterization of biosystem complexity. J. Chem. Inf. Model. 45:1628-1635.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 1628-1635
    • Kavalenka, A.A.1    Filipič, B.2    Hemminga, M.A.3    Štrancar, J.4
  • 27
    • 2942527068 scopus 로고    scopus 로고
    • Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA
    • Columbus, L., and W. L. Hubbell. 2004. Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA. Biochemistry. 43:7273-7287.
    • (2004) Biochemistry , vol.43 , pp. 7273-7287
    • Columbus, L.1    Hubbell, W.L.2
  • 28
    • 0034639884 scopus 로고    scopus 로고
    • High-field EPR studies of the structure and conformational changes of site directed spin labeled bacteriorhodopsin
    • Steinhoff, H. J., A. Savitsky, C. Wegener, M. Pfeiffer, M. Plato, et al. 2000. High-field EPR studies of the structure and conformational changes of site directed spin labeled bacteriorhodopsin. Biochim. Biophys. Acta. 1457:253-262.
    • (2000) Biochim. Biophys. Acta , vol.1457 , pp. 253-262
    • Steinhoff, H.J.1    Savitsky, A.2    Wegener, C.3    Pfeiffer, M.4    Plato, M.5
  • 29
    • 0034132872 scopus 로고    scopus 로고
    • Fast and accurate characterization of biological membranes by EPR spectral simulations of nitroxides
    • Štrancar, J., M. Šentjurc, and M. Schara. 2000. Fast and accurate characterization of biological membranes by EPR spectral simulations of nitroxides. J. Magn. Reson. 142:254-265.
    • (2000) J. Magn. Reson , vol.142 , pp. 254-265
    • Štrancar, J.1    Šentjurc, M.2    Schara, M.3
  • 30
    • 0347995061 scopus 로고    scopus 로고
    • Soft picture of lateral heterogeneity in biomembranes
    • Štrancar, J., T. Koklič, and Z. Arsov. 2003. Soft picture of lateral heterogeneity in biomembranes. J. Membr. Biol. 196:135-146.
    • (2003) J. Membr. Biol , vol.196 , pp. 135-146
    • Štrancar, J.1    Koklič, T.2    Arsov, Z.3
  • 31
    • 34548688208 scopus 로고    scopus 로고
    • A specific binding site for neoxanthin in the monomeric antenna proteins CP26 and CP29 of Photosystem II
    • Caffarri, S., F. Passarini, R. Bassi, and R. Croce. 2007. A specific binding site for neoxanthin in the monomeric antenna proteins CP26 and CP29 of Photosystem II. FEBS Lett. 581:4704-4710.
    • (2007) FEBS Lett , vol.581 , pp. 4704-4710
    • Caffarri, S.1    Passarini, F.2    Bassi, R.3    Croce, R.4
  • 32
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen, H., B. Finkenzeller, and N. Kühlein. 1993. Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem. 215:809-816.
    • (1993) Eur. J. Biochem , vol.215 , pp. 809-816
    • Paulsen, H.1    Finkenzeller, B.2    Kühlein, N.3
  • 33
    • 33846587373 scopus 로고    scopus 로고
    • Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll-a/b protein (LHCIIb)
    • Horn, R., G. Grundmann, and H. Paulsen. 2007. Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll-a/b protein (LHCIIb). J. Mol. Biol. 366:1045-1054.
    • (2007) J. Mol. Biol , vol.366 , pp. 1045-1054
    • Horn, R.1    Grundmann, G.2    Paulsen, H.3
  • 34
    • 0026501332 scopus 로고
    • Spectroscopic properties of LHC-II, the main light-harvesting chlorophyll a/b protein complex from chloroplast membranes
    • Hemelrijk, P. W., S. L. S. Kwa, R. van Grondelle, and J. P. Dekker. 1992. Spectroscopic properties of LHC-II, the main light-harvesting chlorophyll a/b protein complex from chloroplast membranes. Biochim. Biophys. Acta. 1098:159-166.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 159-166
    • Hemelrijk, P.W.1    Kwa, S.L.S.2    van Grondelle, R.3    Dekker, J.P.4
  • 35
    • 0034300084 scopus 로고    scopus 로고
    • Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study
    • Gradinaru, C. C., I. H. M. van Stokkum, A. A. Pascal, R. van Grondelle, and H. van Amerongen. 2000. Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study. J. Phys. Chem. B. 104:9330-9342.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9330-9342
    • Gradinaru, C.C.1    van Stokkum, I.H.M.2    Pascal, A.A.3    van Grondelle, R.4    van Amerongen, H.5
  • 36
    • 0040296635 scopus 로고    scopus 로고
    • Spectroscopic characterization of the spinach Lhcb4 protein (CP29), a minor light-harvesting complex of photosystem II
    • Pascal, A., C. Gradinaru, U. Wacker, E. Peterman, F. Calkoen, et al. 1999. Spectroscopic characterization of the spinach Lhcb4 protein (CP29), a minor light-harvesting complex of photosystem II. Eur. J. Biochem. 262:817-823.
    • (1999) Eur. J. Biochem , vol.262 , pp. 817-823
    • Pascal, A.1    Gradinaru, C.2    Wacker, U.3    Peterman, E.4    Calkoen, F.5
  • 37
    • 52949110565 scopus 로고    scopus 로고
    • Photoprotection in higher plants: The putative quenching site is conserved in all outer light-harvesting complexes of photosystem II
    • Mozzo, M., F. Passarini, R. Bassi, H. van Amerongen, and R. Croce. 2008. Photoprotection in higher plants: The putative quenching site is conserved in all outer light-harvesting complexes of photosystem II. Biochim. Biophys. Acta. 1777:1263-1267.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1263-1267
    • Mozzo, M.1    Passarini, F.2    Bassi, R.3    van Amerongen, H.4    Croce, R.5
  • 38
    • 44449172118 scopus 로고    scopus 로고
    • Photoprotection in the antenna complexes of photosystem II: Role of individual xanthophylls in chlorophyll triplet quenching
    • Mozzo, M., L. Dall'Osto, R. Hienerwadel, R. Bassi, and R. Croce. 2008. Photoprotection in the antenna complexes of photosystem II: role of individual xanthophylls in chlorophyll triplet quenching. J. Biol. Chem. 283:6184-6192.
    • (2008) J. Biol. Chem , vol.283 , pp. 6184-6192
    • Mozzo, M.1    Dall'Osto, L.2    Hienerwadel, R.3    Bassi, R.4    Croce, R.5
  • 39
    • 21444441143 scopus 로고    scopus 로고
    • Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurements
    • Jeschke, G., A. Bender, T. Schweikardt, G. Panek, H. Decker, et al. 2005. Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurements. J. Biol. Chem. 280:18623-18630.
    • (2005) J. Biol. Chem , vol.280 , pp. 18623-18630
    • Jeschke, G.1    Bender, A.2    Schweikardt, T.3    Panek, G.4    Decker, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.