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Volumn 113, Issue 2, 2017, Pages 402-414

The Unique Protein-to-Protein Carotenoid Transfer Mechanism

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; BACTERIAL PROTEIN; CAROTENOID; ENHANCED GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN; ORANGE CAROTENOID PROTEIN, SYNECHOCYSTIS;

EID: 85025617746     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2017.06.002     Document Type: Article
Times cited : (37)

References (43)
  • 1
    • 4444227812 scopus 로고    scopus 로고
    • Carotenoid-induced quenching of the phycobilisome fluorescence in photosystem II-deficient mutant of Synechocystis sp
    • Rakhimberdieva, M.G., Stadnichuk, I.N., et al., Karapetyan, N.V., Carotenoid-induced quenching of the phycobilisome fluorescence in photosystem II-deficient mutant of Synechocystis sp. FEBS Lett. 574 (2004), 85–88.
    • (2004) FEBS Lett. , vol.574 , pp. 85-88
    • Rakhimberdieva, M.G.1    Stadnichuk, I.N.2    Karapetyan, N.V.3
  • 2
    • 33745445226 scopus 로고    scopus 로고
    • A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria
    • Wilson, A., Ajlani, G., et al., Kirilovsky, D., A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria. Plant Cell 18 (2006), 992–1007.
    • (2006) Plant Cell , vol.18 , pp. 992-1007
    • Wilson, A.1    Ajlani, G.2    Kirilovsky, D.3
  • 3
    • 50149083653 scopus 로고    scopus 로고
    • A photoactive carotenoid protein acting as light intensity sensor
    • Wilson, A., Punginelli, C., et al., Kirilovsky, D., A photoactive carotenoid protein acting as light intensity sensor. Proc. Natl. Acad. Sci. USA 105 (2008), 12075–12080.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12075-12080
    • Wilson, A.1    Punginelli, C.2    Kirilovsky, D.3
  • 4
    • 80051943328 scopus 로고    scopus 로고
    • In vitro reconstitution of the cyanobacterial photoprotective mechanism mediated by the orange carotenoid protein in Synechocystis PCC 6803
    • Gwizdala, M., Wilson, A., Kirilovsky, D., In vitro reconstitution of the cyanobacterial photoprotective mechanism mediated by the orange carotenoid protein in Synechocystis PCC 6803. Plant Cell 23 (2011), 2631–2643.
    • (2011) Plant Cell , vol.23 , pp. 2631-2643
    • Gwizdala, M.1    Wilson, A.2    Kirilovsky, D.3
  • 5
    • 80755179274 scopus 로고    scopus 로고
    • The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria
    • Kirilovsky, D., Kerfeld, C.A., The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria. Biochim. Biophys. Acta 1817 (2012), 158–166.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 158-166
    • Kirilovsky, D.1    Kerfeld, C.A.2
  • 6
    • 84906306744 scopus 로고    scopus 로고
    • The time course of non-photochemical quenching in phycobilisomes of Synechocystis sp. PCC6803 as revealed by picosecond time-resolved fluorimetry
    • Maksimov, E.G., Schmitt, F.J., et al., Rubin, A.B., The time course of non-photochemical quenching in phycobilisomes of Synechocystis sp. PCC6803 as revealed by picosecond time-resolved fluorimetry. Biochim. Biophys. Acta 1837 (2014), 1540–1547.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 1540-1547
    • Maksimov, E.G.1    Schmitt, F.J.2    Rubin, A.B.3
  • 7
    • 84931569539 scopus 로고    scopus 로고
    • Features of temporal behavior of fluorescence recovery in Synechocystis sp. PCC6803
    • Maksimov, E.G., Klementiev, K.E., et al., Paschenko, V.Z., Features of temporal behavior of fluorescence recovery in Synechocystis sp. PCC6803. Photosynth. Res. 125 (2015), 167–178.
    • (2015) Photosynth. Res. , vol.125 , pp. 167-178
    • Maksimov, E.G.1    Klementiev, K.E.2    Paschenko, V.Z.3
  • 8
    • 85002388928 scopus 로고    scopus 로고
    • Cyanobacterial photoprotection by the orange carotenoid protein
    • Kirilovsky, D., Kerfeld, C.A., Cyanobacterial photoprotection by the orange carotenoid protein. Nat Plants, 2, 2016, 16180.
    • (2016) Nat Plants , vol.2 , pp. 16180
    • Kirilovsky, D.1    Kerfeld, C.A.2
  • 9
    • 0037226278 scopus 로고    scopus 로고
    • The crystal structure of a cyanobacterial water-soluble carotenoid binding protein
    • Kerfeld, C.A., Sawaya, M.R., et al., Yeates, T.O., The crystal structure of a cyanobacterial water-soluble carotenoid binding protein. Structure 11 (2003), 55–65.
    • (2003) Structure , vol.11 , pp. 55-65
    • Kerfeld, C.A.1    Sawaya, M.R.2    Yeates, T.O.3
  • 10
    • 52949146331 scopus 로고    scopus 로고
    • Occurrence and function of the orange carotenoid protein in photoprotective mechanisms in various cyanobacteria
    • Boulay, C., Abasova, L., et al., Kirilovsky, D., Occurrence and function of the orange carotenoid protein in photoprotective mechanisms in various cyanobacteria. Biochim. Biophys. Acta 1777 (2008), 1344–1354.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1344-1354
    • Boulay, C.1    Abasova, L.2    Kirilovsky, D.3
  • 11
    • 84896893249 scopus 로고    scopus 로고
    • Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection
    • Leverenz, R.L., Jallet, D., et al., Kerfeld, C.A., Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection. Plant Cell 26 (2014), 426–437.
    • (2014) Plant Cell , vol.26 , pp. 426-437
    • Leverenz, R.L.1    Jallet, D.2    Kerfeld, C.A.3
  • 12
    • 78650936291 scopus 로고    scopus 로고
    • Essential role of two tyrosines and two tryptophans on the photoprotection activity of the orange carotenoid protein
    • Wilson, A., Punginelli, C., et al., Kirilovsky, D., Essential role of two tyrosines and two tryptophans on the photoprotection activity of the orange carotenoid protein. Biochim. Biophys. Acta 1807 (2011), 293–301.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 293-301
    • Wilson, A.1    Punginelli, C.2    Kirilovsky, D.3
  • 13
    • 84966560284 scopus 로고    scopus 로고
    • A comparative study of three signaling forms of the orange carotenoid protein
    • Maksimov, E.G., Moldenhauer, M., et al., Rubin, A.B., A comparative study of three signaling forms of the orange carotenoid protein. Photosynth. Res. 130 (2016), 389–401.
    • (2016) Photosynth. Res. , vol.130 , pp. 389-401
    • Maksimov, E.G.1    Moldenhauer, M.2    Rubin, A.B.3
  • 14
    • 84992195231 scopus 로고    scopus 로고
    • 288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP
    • 288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP. Biochim. Biophys. Acta 1858 (2017), 1–11.
    • (2017) Biochim. Biophys. Acta , vol.1858 , pp. 1-11
    • Sluchanko, N.N.1    Klementiev, K.E.2    Maksimov, E.G.3
  • 15
    • 84938543605 scopus 로고    scopus 로고
    • The signaling state of orange carotenoid protein
    • Maksimov, E.G., Shirshin, E.A., et al., Rubin, A.B., The signaling state of orange carotenoid protein. Biophys. J. 109 (2015), 595–607.
    • (2015) Biophys. J. , vol.109 , pp. 595-607
    • Maksimov, E.G.1    Shirshin, E.A.2    Rubin, A.B.3
  • 16
    • 84940911120 scopus 로고    scopus 로고
    • Regulation of orange carotenoid protein activity in cyanobacterial photoprotection
    • Thurotte, A., Lopez-Igual, R., et al., Kirilovsky, D., Regulation of orange carotenoid protein activity in cyanobacterial photoprotection. Plant Physiol. 169 (2015), 737–747.
    • (2015) Plant Physiol. , vol.169 , pp. 737-747
    • Thurotte, A.1    Lopez-Igual, R.2    Kirilovsky, D.3
  • 17
    • 84964555793 scopus 로고    scopus 로고
    • Native mass spectrometry and ion mobility characterize the orange carotenoid protein functional domains
    • Zhang, H., Liu, H., et al., Blankenship, R.E., Native mass spectrometry and ion mobility characterize the orange carotenoid protein functional domains. Biochim. Biophys. Acta. 1857 (2016), 734–739.
    • (2016) Biochim. Biophys. Acta. , vol.1857 , pp. 734-739
    • Zhang, H.1    Liu, H.2    Blankenship, R.E.3
  • 18
    • 84944080519 scopus 로고    scopus 로고
    • Local and global structural drivers for the photoactivation of the orange carotenoid protein
    • Gupta, S., Guttman, M., et al., Kerfeld, C.A., Local and global structural drivers for the photoactivation of the orange carotenoid protein. Proc. Natl. Acad. Sci. USA 112 (2015), E5567–E5574.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. E5567-E5574
    • Gupta, S.1    Guttman, M.2    Kerfeld, C.A.3
  • 19
    • 84933564631 scopus 로고    scopus 로고
    • Photosynthesis. A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection
    • Leverenz, R.L., Sutter, M., et al., Kerfeld, C.A., Photosynthesis. A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection. Science 348 (2015), 1463–1466.
    • (2015) Science , vol.348 , pp. 1463-1466
    • Leverenz, R.L.1    Sutter, M.2    Kerfeld, C.A.3
  • 20
    • 85008646183 scopus 로고    scopus 로고
    • Fluorescent labeling preserving OCP photoactivity reveals its reorganization during the photocycle
    • Maksimov, E.G., Sluchanko, N.N., et al., Rubin, A.B., Fluorescent labeling preserving OCP photoactivity reveals its reorganization during the photocycle. Biophys. J. 112 (2017), 46–56.
    • (2017) Biophys. J. , vol.112 , pp. 46-56
    • Maksimov, E.G.1    Sluchanko, N.N.2    Rubin, A.B.3
  • 22
    • 78249236871 scopus 로고    scopus 로고
    • Excited-state properties of the 16-kDa red carotenoid protein from Arthrospira maxima
    • Chábera, P., Durchan, M., et al., Polívka, T., Excited-state properties of the 16-kDa red carotenoid protein from Arthrospira maxima. Biochim. Biophys. Acta 1807 (2011), 30–35.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 30-35
    • Chábera, P.1    Durchan, M.2    Polívka, T.3
  • 23
    • 84977581459 scopus 로고    scopus 로고
    • Different functions of the paralogs to the N-terminal domain of the orange carotenoid protein in the cyanobacterium Anabaena sp. PCC 7120
    • López-Igual, R., Wilson, A., et al., Kirilovsky, D., Different functions of the paralogs to the N-terminal domain of the orange carotenoid protein in the cyanobacterium Anabaena sp. PCC 7120. Plant Physiol. 171 (2016), 1852–1866.
    • (2016) Plant Physiol. , vol.171 , pp. 1852-1866
    • López-Igual, R.1    Wilson, A.2    Kirilovsky, D.3
  • 24
    • 84991728641 scopus 로고    scopus 로고
    • Structure, diversity, and evolution of a new family of soluble carotenoid-binding proteins in cyanobacteria
    • Melnicki, M.R., Leverenz, R.L., et al., Kerfeld, C.A., Structure, diversity, and evolution of a new family of soluble carotenoid-binding proteins in cyanobacteria. Mol. Plant 9 (2016), 1379–1394.
    • (2016) Mol. Plant , vol.9 , pp. 1379-1394
    • Melnicki, M.R.1    Leverenz, R.L.2    Kerfeld, C.A.3
  • 25
    • 85013117524 scopus 로고    scopus 로고
    • Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism
    • Moldenhauer, M., Sluchanko, N.N., et al., Friedrich, T., Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism. Photosynth. Res., 2017, 10.1007/s11120-017-0353-3.
    • (2017) Photosynth. Res.
    • Moldenhauer, M.1    Sluchanko, N.N.2    Friedrich, T.3
  • 26
    • 84901400843 scopus 로고    scopus 로고
    • The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher
    • Sedoud, A., López-Igual, R., et al., Kirilovsky, D., The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher. Plant Cell 26 (2014), 1781–1791.
    • (2014) Plant Cell , vol.26 , pp. 1781-1791
    • Sedoud, A.1    López-Igual, R.2    Kirilovsky, D.3
  • 27
    • 85013832143 scopus 로고    scopus 로고
    • Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein
    • Moldenhauer, M., Sluchanko, N.N., et al., Friedrich, T., Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein. Photosynth. Res., 2017, 10.1007/s11120-017-0346-2.
    • (2017) Photosynth. Res.
    • Moldenhauer, M.1    Sluchanko, N.N.2    Friedrich, T.3
  • 28
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W., Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005), 207–234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 29
    • 0014629135 scopus 로고
    • The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin
    • Schaub, M.C., Perry, S.V., The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin. Biochem. J. 115 (1969), 993–1004.
    • (1969) Biochem. J. , vol.115 , pp. 993-1004
    • Schaub, M.C.1    Perry, S.V.2
  • 30
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: a Windows PC-based system for small-angle scattering data analysis
    • Konarev, P.V., Volkov, V.V., et al., Svergun, D.I., PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Cryst. 36 (2003), 1277–1282.
    • (2003) J. Appl. Cryst. , vol.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Svergun, D.I.3
  • 31
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D.I., Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25 (1992), 495–503.
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 32
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D., Svergun, D.I., DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Cryst. 42 (2009), 342–346.
    • (2009) J. Appl. Cryst. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 33
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V., Svergun, D.I., Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Cryst. 36 (2003), 860–864.
    • (2003) J. Appl. Cryst. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 34
    • 0029185933 scopus 로고
    • CRYSOL—a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., Koch, M.H.J., CRYSOL—a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28 (1995), 768–773.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 35
    • 85020692029 scopus 로고    scopus 로고
    • Photoactivation mechanism of a carotenoid-based photoreceptor
    • Bandara, S., Ren, Z., et al., Yang, X., Photoactivation mechanism of a carotenoid-based photoreceptor. Proc. Natl. Acad. Sci. USA., 2017, 10.1073/pnas.1700956114.
    • (2017) Proc. Natl. Acad. Sci. USA.
    • Bandara, S.1    Ren, Z.2    Yang, X.3
  • 36
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov, M.V., Franke, D., et al., Svergun, D.I., New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Cryst. 45 (2012), 342–350.
    • (2012) J. Appl. Cryst. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1    Franke, D.2    Svergun, D.I.3
  • 37
    • 0030736114 scopus 로고    scopus 로고
    • Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution
    • Ben-Tal, N., Sitkoff, D., et al., Honig, B., Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution. J. Phys. Chem. B 101 (1997), 450–457.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 450-457
    • Ben-Tal, N.1    Sitkoff, D.2    Honig, B.3
  • 38
    • 85017162864 scopus 로고    scopus 로고
    • Biophysical modeling of in vitro and in vivo processes underlying regulated photoprotective mechanism in cyanobacteria
    • Shirshin, E.A., Nikonova, E.E., et al., Maksimov, E.G., Biophysical modeling of in vitro and in vivo processes underlying regulated photoprotective mechanism in cyanobacteria. Photosynth. Res., 2017, 10.1007/s11120-017-0377-8.
    • (2017) Photosynth. Res.
    • Shirshin, E.A.1    Nikonova, E.E.2    Maksimov, E.G.3
  • 39
    • 85020013234 scopus 로고    scopus 로고
    • Deletion of the short N-terminal extension in OCP reveals the main site for FRP binding
    • Sluchanko, N.N., Slonimskiy, Y.B., et al., Maksimov, E.G., Deletion of the short N-terminal extension in OCP reveals the main site for FRP binding. FEBS Lett., 2017, 10.1002/1873-3468.12680.
    • (2017) FEBS Lett.
    • Sluchanko, N.N.1    Slonimskiy, Y.B.2    Maksimov, E.G.3
  • 40
    • 84892581204 scopus 로고    scopus 로고
    • Molecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein
    • Zhang, H., Liu, H., et al., Blankenship, R.E., Molecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein. Biochemistry 53 (2014), 13–19.
    • (2014) Biochemistry , vol.53 , pp. 13-19
    • Zhang, H.1    Liu, H.2    Blankenship, R.E.3
  • 41
    • 77953313030 scopus 로고    scopus 로고
    • Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria
    • Wilson, A., Kinney, J.N., et al., Kerfeld, C.A., Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria. J. Biol. Chem. 285 (2010), 18364–18375.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18364-18375
    • Wilson, A.1    Kinney, J.N.2    Kerfeld, C.A.3
  • 42
    • 85016935912 scopus 로고    scopus 로고
    • Native mass spectrometry analysis of oligomerization states of fluorescence recovery protein and orange carotenoid protein: two proteins involved in the cyanobacterial photoprotection cycle
    • Lu, Y., Liu, H., et al., Blankenship, R.E., Native mass spectrometry analysis of oligomerization states of fluorescence recovery protein and orange carotenoid protein: two proteins involved in the cyanobacterial photoprotection cycle. Biochemistry 56 (2017), 160–166.
    • (2017) Biochemistry , vol.56 , pp. 160-166
    • Lu, Y.1    Liu, H.2    Blankenship, R.E.3
  • 43
    • 79953206938 scopus 로고    scopus 로고
    • Identification of STARD3 as a lutein-binding protein in the macula of the primate retina
    • Li, B., Vachali, P., et al., Bernstein, P.S., Identification of STARD3 as a lutein-binding protein in the macula of the primate retina. Biochemistry 50 (2011), 2541–2549.
    • (2011) Biochemistry , vol.50 , pp. 2541-2549
    • Li, B.1    Vachali, P.2    Bernstein, P.S.3


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