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Volumn 48, Issue 2-3, 1999, Pages 120-126

Photosystem II activity and turnover of the D1 protein are impaired in the psbA Y112L mutant of Synechocystis PCC6803 sp.

Author keywords

Cyanobacteria; Photosystem II; Site directed mutagenesis

Indexed keywords

BACTERIAL PROTEIN;

EID: 0010265962     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(99)00040-8     Document Type: Conference Paper
Times cited : (6)

References (34)
  • 1
    • 0024769579 scopus 로고
    • Molecular analysis of psbA mutations responsible for various herbicide resistance phenotypes in Synechocystis 6714
    • [1] G. Ajlani, D. Kirilovsky, M. Picaud, C. Astier, Molecular analysis of psbA mutations responsible for various herbicide resistance phenotypes in Synechocystis 6714, Plant Mol. Biol. 13 (1989) 469-479.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 469-479
    • Ajlani, G.1    Kirilovsky, D.2    Picaud, M.3    Astier, C.4
  • 3
    • 0026453128 scopus 로고
    • Role of the carboxy terminus of polypeptide D1 in the assembly of a functional water-oxidizing manganese cluster in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Assembly requires a free carboxyl group at C-terminal position 344
    • [3] P.J. Nixon, J.T. Trost, B.A. Diner, Role of the carboxy terminus of polypeptide D1 in the assembly of a functional water-oxidizing manganese cluster in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: assembly requires a free carboxyl group at C-terminal position 344, Biochemistry 31 (1992) 10859-10871.
    • (1992) Biochemistry , vol.31 , pp. 10859-10871
    • Nixon, P.J.1    Trost, J.T.2    Diner, B.A.3
  • 4
    • 0026828658 scopus 로고
    • Mutations in the D1 subunit of Photosystem II distinguish between quinone and herbicide binding sites
    • [4] N. Ohad, J. Hirschberg, Mutations in the D1 subunit of Photosystem II distinguish between quinone and herbicide binding sites, Plant Cell 4 (1992) 273-282.
    • (1992) Plant Cell , vol.4 , pp. 273-282
    • Ohad, N.1    Hirschberg, J.2
  • 5
    • 0028445692 scopus 로고
    • Changes of amino acid sequence in PEST-like area and QEEET motif affect degradation rate of D1 polypeptide in photosystem II
    • [5] T. Tyystjärvi, E.-M. Aro, C. Jansson, P. Mäenpää, Changes of amino acid sequence in PEST-like area and QEEET motif affect degradation rate of D1 polypeptide in photosystem II, Plant Mol. Biol. 25 (1994) 517-526.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 517-526
    • Tyystjärvi, T.1    Aro, E.-M.2    Jansson, C.3    Mäenpää, P.4
  • 6
    • 0027572143 scopus 로고
    • Protein modification in the D2 protein of Photosystem II affects properties of the QB/herbicide binding environment
    • [6] H. Kless, M. Oren-Shamir, I. Ohad, M. Edelman, W. Vermaas, Protein modification in the D2 protein of Photosystem II affects properties of the QB/herbicide binding environment, Z. Naturforsch. 48c (1993) 185-190.
    • (1993) Z. Naturforsch. , vol.48 C , pp. 185-190
    • Kless, H.1    Oren-Shamir, M.2    Ohad, I.3    Edelman, M.4    Vermaas, W.5
  • 8
    • 0028902008 scopus 로고
    • Many combinations of amino acid sequence in a conserved region of the D1 protein satisfy photosystem II function
    • [8] H. Kless, W. Vermaas, Many combinations of amino acid sequence in a conserved region of the D1 protein satisfy photosystem II function, J. Mol. Biol. 246 (1995) 120-131.
    • (1995) J. Mol. Biol. , vol.246 , pp. 120-131
    • Kless, H.1    Vermaas, W.2
  • 10
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • [10] J. Deisenhofer, O. Epp, K. Kiki, R. Huber, H. Michel, Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution, Nature 318 (1985) 618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Kiki, K.3    Huber, R.4    Michel, H.5
  • 11
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • [11] J.P. Allen, G. Feher, T.O. Yeates, H. Komiya, D.C. Rees, Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits, Proc. Natl. Acad. Sci. USA 84 (1987) 6162-6166.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 12
    • 0025281016 scopus 로고
    • Light-dependent D1 protein synthesis and translocation is regulated by reaction center II
    • [12] N. Adir, S. Shochat, I. Ohad, Light-dependent D1 protein synthesis and translocation is regulated by reaction center II, J. Biol. Chem. 265 (1990) 12563-12568.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12563-12568
    • Adir, N.1    Shochat, S.2    Ohad, I.3
  • 13
    • 0000226607 scopus 로고
    • Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes
    • J. Barber (Ed.), Elsevier, Amsterdam
    • [13] O. Prasil, N. Adir, I. Ohad, Dynamics of photosystem II: mechanism of photoinhibition and recovery processes, in: J. Barber (Ed.), The Photosystems: Structure, Function and Molecular Biology, Elsevier, Amsterdam, 1992, pp. 295-348.
    • (1992) The Photosystems: Structure, Function and Molecular Biology , pp. 295-348
    • Prasil, O.1    Adir, N.2    Ohad, I.3
  • 14
    • 0023658397 scopus 로고
    • Mechanism for the accelerated degradation of intracellular proteins after limited damage by free radicals
    • [14] R.T.A. Dean, Mechanism for the accelerated degradation of intracellular proteins after limited damage by free radicals, FEBS Lett. 220 (1987) 278-282.
    • (1987) FEBS Lett. , vol.220 , pp. 278-282
    • Dean, R.T.A.1
  • 17
    • 0000561603 scopus 로고
    • Oxygen evolution
    • Kluwer, Dordrecht
    • [17] D. Britt, Oxygen evolution, in: Oxygenic Photosynthesis, Kluwer, Dordrecht, 1995, pp. 137-164.
    • (1995) Oxygenic Photosynthesis , pp. 137-164
    • Britt, D.1
  • 18
    • 0026215160 scopus 로고
    • Sequence analysis of the D1 and D2 reaction center proteins of Photosystem II
    • [18] B. Svensson, I. Vass, S. Styring, Sequence analysis of the D1 and D2 reaction center proteins of Photosystem II, Z. Naturforsch. 46c (1991) 765-776.
    • (1991) Z. Naturforsch. , vol.46 C , pp. 765-776
    • Svensson, B.1    Vass, I.2    Styring, S.3
  • 19
    • 0025298292 scopus 로고
    • Structure of donor side components in photosystem II predicted by computer modeling
    • [19] B. Svensson, I. Vass, E. Cedergeren, S. Styring, Structure of donor side components in photosystem II predicted by computer modeling, EMBO J. 9 (1990) 2051-2059.
    • (1990) EMBO J. , vol.9 , pp. 2051-2059
    • Svensson, B.1    Vass, I.2    Cedergeren, E.3    Styring, S.4
  • 20
    • 0023781850 scopus 로고
    • Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system
    • [20] R.J. Debus, B.A. Barry, G.T. Babcock, L. McIntosh, Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system, Proc. Natl. Acad. Sci. USA 85 (1988) 427-430.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 427-430
    • Debus, R.J.1    Barry, B.A.2    Babcock, G.T.3    McIntosh, L.4
  • 21
    • 45449121949 scopus 로고
    • Changes in the properties of reaction center II during the initial stages of photoinhibition as revealed by thermoluminescence measurements
    • [21] I. Ohad, H. Koike, S. Shochat, Y. Inoue, Changes in the properties of reaction center II during the initial stages of photoinhibition as revealed by thermoluminescence measurements, Biochim. Biophys. Acta 933 (1988) 288-298.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 288-298
    • Ohad, I.1    Koike, H.2    Shochat, S.3    Inoue, Y.4
  • 22
    • 0029015587 scopus 로고
    • Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation
    • [22] H. Zer, I. Ohad, Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation, Eur. J. Biochem. 231 (1995) 448-453.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 448-453
    • Zer, H.1    Ohad, I.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • [24] U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 85047693636 scopus 로고
    • Turnover of thylakoid photosystem II proteins during photoinhibition of Chlamydomonas reinhardtii
    • [25] G. Schuster, R. Timberg, I. Ohad, Turnover of thylakoid photosystem II proteins during photoinhibition of Chlamydomonas reinhardtii, Eur. J. Biochem. 177 (1988) 403-410.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 403-410
    • Schuster, G.1    Timberg, R.2    Ohad, I.3
  • 26
    • 84989751883 scopus 로고
    • Thermoluminescence in plants
    • [26] S. Demeter, Govindjee, Thermoluminescence in plants, Physiol. Plant. 75 (1989) 121-130.
    • (1989) Physiol. Plant. , vol.75 , pp. 121-130
    • Demeter, S.1    Govindjee2
  • 27
    • 0000932850 scopus 로고    scopus 로고
    • Heterogeneity and photoinhibition of photosystem II studied with thermoluminescence
    • [27] S. Andree, E. Weis, A. Krieger, Heterogeneity and photoinhibition of photosystem II studied with thermoluminescence, Plant Physiol. 116 (1998) 1053-1061.
    • (1998) Plant Physiol. , vol.116 , pp. 1053-1061
    • Andree, S.1    Weis, E.2    Krieger, A.3
  • 28
    • 0028985845 scopus 로고
    • Rapid turnover of the RCII-D1 protein in the dark is induced by photoinactivation of photosystem II in Scenedesmus wt and the PSII-donor defective LF-1 mutant cells
    • [28] H. Gong, I. Ohad, Rapid turnover of the RCII-D1 protein in the dark is induced by photoinactivation of photosystem II in Scenedesmus wt and the PSII-donor defective LF-1 mutant cells, Biochim. Biophys. Acta 1228 (1995) 181-188.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 181-188
    • Gong, H.1    Ohad, I.2
  • 29
    • 0028155831 scopus 로고
    • Photosystem II in a mutant of Chlamydomonas reinhardtii lacking 23 kDa psbP protein shows increased sensitivity to photoinhibition in the absence of chloride
    • [29] M. Rova, L.-G. Franzen, P.-O. Fredriksson, S. Styring, Photosystem II in a mutant of Chlamydomonas reinhardtii lacking 23 kDa psbP protein shows increased sensitivity to photoinhibition in the absence of chloride, Photosynth. Res. 39 (1994) 75-83.
    • (1994) Photosynth. Res. , vol.39 , pp. 75-83
    • Rova, M.1    Franzen, L.-G.2    Fredriksson, P.-O.3    Styring, S.4
  • 30
    • 0026709669 scopus 로고
    • Oxygen yield and thermoluminescence characteristics of a cyanobacterium lacking the manganese-stabilizing protein of Photosystem II
    • [30] R.L. Burnap, J.-R. Shen, P.A. Jurasnic, Y. Inuoe, L.A. Sherman, Oxygen yield and thermoluminescence characteristics of a cyanobacterium lacking the manganese-stabilizing protein of Photosystem II, Biochemistry 31 (1992) 7404-7410.
    • (1992) Biochemistry , vol.31 , pp. 7404-7410
    • Burnap, R.L.1    Shen, J.-R.2    Jurasnic, P.A.3    Inuoe, Y.4    Sherman, L.A.5
  • 31
    • 0342601459 scopus 로고    scopus 로고
    • Comparison of chloride-depleted and calcium-depleted PSII: The midpoint potential of QA and susceptibility to photodamage
    • [31] A. Krieger, A.W. Rutherford, Comparison of chloride-depleted and calcium-depleted PSII: the midpoint potential of QA and susceptibility to photodamage, Biochim. Biophys. Acta 1319 (1997) 91-98.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 91-98
    • Krieger, A.1    Rutherford, A.W.2
  • 32
    • 0026597716 scopus 로고
    • Two sites of primary deg-radation of D1-protein induced by acceptor or donor side photoinhibition in photosystem II core complex
    • [32] J. De Las Rivas, B. Andersson, J. Barber, Two sites of primary deg-radation of D1-protein induced by acceptor or donor side photoinhibition in photosystem II core complex, FEBS Lett. 301 (1992) 246-252.
    • (1992) FEBS Lett. , vol.301 , pp. 246-252
    • De Las Rivas, J.1    Andersson, B.2    Barber, J.3
  • 33
    • 0031717147 scopus 로고    scopus 로고
    • A knowledge-based three-dimensional model of the photosystem II reaction centre of Chlamydomonas reinhardtii
    • [33] J. Xiong, S. Subramaniam, Govindjee, A knowledge-based three-dimensional model of the Photosystem II reaction centre of Chlamydomonas reinhardtii, Photosynth. Res. 56 (1998) 229-254.
    • (1998) Photosynth. Res. , vol.56 , pp. 229-254
    • Xiong, J.1    Subramaniam, S.2    Govindjee3
  • 34
    • 0031028025 scopus 로고    scopus 로고
    • Role of carotene in the rapid turnover and assembly of photosystem II in Chlamydomonas reinhardtii
    • [34] A. Trebst, B. Depka, Role of carotene in the rapid turnover and assembly of photosystem II in Chlamydomonas reinhardtii, FEBS Lett. 400 (1997) 359-362.
    • (1997) FEBS Lett. , vol.400 , pp. 359-362
    • Trebst, A.1    Depka, B.2


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