메뉴 건너뛰기




Volumn 7, Issue MAR2016, 2016, Pages

Synthesis of chlorophyll-binding proteins in a fully segregated δycf54 strain of the cyanobacterium synechocystis PCC 6803

Author keywords

Chlorophyll; Mg protoporphyrin IX methylester cyclase; Photosystem II; Protochlorophyllide; Synechocystis 6803; Ycf54

Indexed keywords


EID: 84961710198     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2016.00292     Document Type: Article
Times cited : (26)

References (52)
  • 1
    • 84870776667 scopus 로고    scopus 로고
    • LCAA, a novel factor required for magnesium protoporphyrin monomethylester cyclase accumulation and feedback control of aminolevulinic acid biosynthesis in Tobacco
    • Albus, C. A., Salinas, A., Czarnecki, O., Kahlau, S., Rothbart, M., Thiele, W., et al. (2012). LCAA, a novel factor required for magnesium protoporphyrin monomethylester cyclase accumulation and feedback control of aminolevulinic acid biosynthesis in Tobacco. Plant Physiol. 160, 1923-1939. doi: 10. 1104/pp. 112. 206045
    • (2012) Plant Physiol , vol.160 , pp. 1923-1939
    • Albus, C.A.1    Salinas, A.2    Czarnecki, O.3    Kahlau, S.4    Rothbart, M.5    Thiele, W.6
  • 3
    • 79955374758 scopus 로고    scopus 로고
    • Investigating the early stages of Photosystem II assembly in Synechocystis sp PCC 6803: Isolation of CP47 and CP43 complexes
    • Boehm, M., Romero, E., Reisinger, V., Yu, J., Komenda, J., Eichacker, L. A., et al. (2011). Investigating the early stages of Photosystem II assembly in Synechocystis sp PCC 6803: isolation of CP47 and CP43 complexes. J. Biol. Chem. 286, 14812-14819. doi: 10. 1074/jbc. M110. 207944
    • (2011) J. Biol. Chem , vol.286 , pp. 14812-14819
    • Boehm, M.1    Romero, E.2    Reisinger, V.3    Yu, J.4    Komenda, J.5    Eichacker, L.A.6
  • 4
    • 84869222276 scopus 로고    scopus 로고
    • Subunit composition of CP43-less photosystem II complexes of Synechocystissp PCC 6803: Implications for the assembly and repair of photosystem II
    • Boehm, M., Yu, J., Reisinger, V., Bečková, M., Eichacker, L. A., Schlodder, E., et al. (2012). Subunit composition of CP43-less photosystem II complexes of Synechocystissp PCC 6803: implications for the assembly and repair of photosystem II. Philos. Trans. R. Soc. B Biol. Sci. 367, 3444-3454. doi: 10. 1098/rstb. 2012. 0066
    • (2012) Philos. Trans. R. Soc. B Biol. Sci , vol.367 , pp. 3444-3454
    • Boehm, M.1    Yu, J.2    Reisinger, V.3    Bečková, M.4    Eichacker, L.A.5    Schlodder, E.6
  • 5
    • 84876186732 scopus 로고    scopus 로고
    • Distribution and origin of oxygen-dependent and oxygen-independent forms of Mg-protoporphyrin monomethylester cyclase among phototrophic proteobacteria
    • Boldareva-Nuianzina, E. N., Bláhová, Z., Sobotka, R., and Koblížek, M. (2013). Distribution and origin of oxygen-dependent and oxygen-independent forms of Mg-protoporphyrin monomethylester cyclase among phototrophic proteobacteria. Appl. Environ. Microbiol. 79, 2596-2604. doi: 10. 1128/AEM. 00104-13
    • (2013) Appl. Environ. Microbiol , vol.79 , pp. 2596-2604
    • Boldareva-Nuianzina, E.N.1    Bláhová, Z.2    Sobotka, R.3    Koblížek, M.4
  • 6
    • 84901233802 scopus 로고    scopus 로고
    • The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)
    • Bollivar, D., Braumann, I., Berendt, K., Gough, S. P., and Hansson, M. (2014). The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.). FEBS J. 281, 2377-2386. doi: 10. 1111/febs. 12790
    • (2014) FEBS J , vol.281 , pp. 2377-2386
    • Bollivar, D.1    Braumann, I.2    Berendt, K.3    Gough, S.P.4    Hansson, M.5
  • 7
    • 84874037609 scopus 로고    scopus 로고
    • Identification of an 8-vinyl reductase involved in bacteriochlorophyll biosynthesis inRhodobacter sphaeroides and evidence for the existence of a third distinct class of the enzyme
    • Canniffe, D. P., Jackson, P. J., Hollingshead, S., Dickman, M. J., and Hunter, C. N. (2013). Identification of an 8-vinyl reductase involved in bacteriochlorophyll biosynthesis inRhodobacter sphaeroides and evidence for the existence of a third distinct class of the enzyme. Biochem. J. 450, 397-405. doi: 10. 1042/BJ20121723
    • (2013) Biochem. J , vol.450 , pp. 397-405
    • Canniffe, D.P.1    Jackson, P.J.2    Hollingshead, S.3    Dickman, M.J.4    Hunter, C.N.5
  • 8
    • 84899146539 scopus 로고    scopus 로고
    • A cyanobacterial chlorophyll synthase-HliD complex associates with the Ycf39 protein and the YidC/Alb3 insertase
    • Chidgey, J. W., Linhartová, M., Komenda, J., Jackson, P. J., Dickman, M. J., Canniffe, D. P., et al. (2014). A cyanobacterial chlorophyll synthase-HliD complex associates with the Ycf39 protein and the YidC/Alb3 insertase. Plant Cell 26, 1267-1279. doi: 10. 1105/tpc. 114. 124495
    • (2014) Plant Cell , vol.26 , pp. 1267-1279
    • Chidgey, J.W.1    Linhartová, M.2    Komenda, J.3    Jackson, P.J.4    Dickman, M.J.5    Canniffe, D.P.6
  • 9
    • 0017171618 scopus 로고
    • Periodic variations in the ratio of free to thylakoid-bound chloroplast ribosomes during the cell cycle ofChlamydomonas reinhardtii
    • Chua, N. H., Blobel, G., Siekevitz, P., and Palade, G. E. (1976). Periodic variations in the ratio of free to thylakoid-bound chloroplast ribosomes during the cell cycle ofChlamydomonas reinhardtii. J. Cell Biol. 71, 497-514. doi: 10. 1083/jcb. 71. 2. 497
    • (1976) J. Cell Biol , vol.71 , pp. 497-514
    • Chua, N.H.1    Blobel, G.2    Siekevitz, P.3    Palade, G.E.4
  • 10
    • 60249085223 scopus 로고    scopus 로고
    • Psb28 protein is involved in the biogenesis of the photosystem II inner antenna CP47 (PsbB) in the cyanobacterium Synechocystis sp. PCC 6803
    • Dobáková, M., Sobotka, R., Tichý, M., and Komenda, J. (2009). Psb28 protein is involved in the biogenesis of the photosystem II inner antenna CP47 (PsbB) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 149, 1076-1086. doi: 10. 1104/pp. 108. 130039
    • (2009) Plant Physiol , vol.149 , pp. 1076-1086
    • Dobáková, M.1    Sobotka, R.2    Tichý, M.3    Komenda, J.4
  • 11
    • 0026515088 scopus 로고
    • Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts
    • Eichacker, L., Paulsen, H., and Rüdiger, W. (1992). Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts. Eur. J. Biochem. 205, 17-24. doi: 10. 1111/j. 1432-1033. 1992. tb16747. x
    • (1992) Eur. J. Biochem , vol.205 , pp. 17-24
    • Eichacker, L.1    Paulsen, H.2    Rüdiger, W.3
  • 12
    • 0029751135 scopus 로고    scopus 로고
    • Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 by chlorophyll a or Zn-pheophytin a
    • Eichacker, L. A., Helfrich, M., Rüdiger, W., and Muller, B. (1996). Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 by chlorophyll a or Zn-pheophytin a. J. Biol. Chem. 271, 32174-32179. doi: 10. 1074/jbc. 271. 50. 32174
    • (1996) J. Biol. Chem , vol.271 , pp. 32174-32179
    • Eichacker, L.A.1    Helfrich, M.2    Rüdiger, W.3    Muller, B.4
  • 13
    • 84864280543 scopus 로고    scopus 로고
    • Non-enzymatic conversion of chlorophyll-a into chlorophyll-d in vitro: A model oxidation pathway for chlorophyll-d biosynthesis
    • Fukusumi, T., Matsuda, K., Mizoguchi, T., Miyatake, T., Ito, S., Ikeda, T., et al. (2012). Non-enzymatic conversion of chlorophyll-a into chlorophyll-d in vitro: a model oxidation pathway for chlorophyll-d biosynthesis. FEBS Lett. 586, 2338-2341. doi: 10. 1016/j. febslet. 2012. 05. 036
    • (2012) FEBS Lett , vol.586 , pp. 2338-2341
    • Fukusumi, T.1    Matsuda, K.2    Mizoguchi, T.3    Miyatake, T.4    Ito, S.5    Ikeda, T.6
  • 14
    • 84865015496 scopus 로고    scopus 로고
    • Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase inSynechocystis PCC 6803
    • Hollingshead, S., Kopečná, J., Jackson, P. J., Canniffe, D. P., Davison, P. A., Dickman, M. J., et al. (2012). Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase inSynechocystis PCC 6803. J. Biol. Chem. 287, 27823-27833. doi: 10. 1074/jbc. M112. 352526
    • (2012) J. Biol. Chem , vol.287 , pp. 27823-27833
    • Hollingshead, S.1    Kopečná, J.2    Jackson, P.J.3    Canniffe, D.P.4    Davison, P.A.5    Dickman, M.J.6
  • 15
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2. 5 Å resolution
    • Jordan, P., Fromme, P., Witt, H. T., Klukas, O., Saenger, W., and Krauss, N. (2001). Three-dimensional structure of cyanobacterial photosystem I at 2. 5 Å resolution. Nature 411, 909-917. doi: 10. 1038/35082000
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 16
    • 0017724572 scopus 로고
    • A new spectrophotometric assay for protein in cell extracts
    • Kalb, V. F., and Bernlohr, R. W. (1977). A new spectrophotometric assay for protein in cell extracts. Anal. Biochem. 82, 362-371. doi: 10. 1016/0003-2697(77)90173-7
    • (1977) Anal. Biochem , vol.82 , pp. 362-371
    • Kalb, V.F.1    Bernlohr, R.W.2
  • 17
    • 84863115403 scopus 로고    scopus 로고
    • Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803
    • Kanesaki, Y., Shiwa, Y., Tajima, N., Suzuki, M., Watanabe, S., Sato, N., et al. (2012). Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803. DNA Res. 19, 67-79. doi: 10. 1093/dnares/dsr042
    • (2012) DNA Res , vol.19 , pp. 67-79
    • Kanesaki, Y.1    Shiwa, Y.2    Tajima, N.3    Suzuki, M.4    Watanabe, S.5    Sato, N.6
  • 18
    • 84856217923 scopus 로고    scopus 로고
    • FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is physically linked to the final steps of the Mg++-branch of this pathway
    • Kauss, D., Bischof, S., Steiner, S., Apel, K., and Meskauskiene, R. (2012). FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is physically linked to the final steps of the Mg++-branch of this pathway. FEBS Lett. 586, 211-216. doi: 10. 1016/j. febslet. 2011. 12. 029
    • (2012) FEBS Lett , vol.586 , pp. 211-216
    • Kauss, D.1    Bischof, S.2    Steiner, S.3    Apel, K.4    Meskauskiene, R.5
  • 19
    • 0030743251 scopus 로고    scopus 로고
    • Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method
    • Ke, S. H., and Madison, E. L. (1997). Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method. Nucleic Acids Res. 25, 3371-3372. doi: 10. 1093/nar/25. 16. 3371
    • (1997) Nucleic Acids Res , vol.25 , pp. 3371-3372
    • Ke, S.H.1    Madison, E.L.2
  • 20
    • 84899148914 scopus 로고    scopus 로고
    • Discovery of a chlorophyll binding protein complex involved in the early steps of photosystem II assembly in Synechocystis
    • Knoppová, J., Sobotka, R., Tichý, M., Yu, J., Koník, P., Halada, P., et al. (2014). Discovery of a chlorophyll binding protein complex involved in the early steps of photosystem II assembly in Synechocystis. Plant Cell 26, 1200-1212. doi: 10. 1105/tpc. 114. 123919
    • (2014) Plant Cell , vol.26 , pp. 1200-1212
    • Knoppová, J.1    Sobotka, R.2    Tichý, M.3    Yu, J.4    Koník, P.5    Halada, P.6
  • 22
    • 53049083938 scopus 로고    scopus 로고
    • The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystem II in Synechocystis sp PCC 6803
    • Komenda, J., Nickelsen, J., Tichý, M., Prášil, O., Eichacker, L. A., and Nixon, P. J. (2008). The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystem II in Synechocystis sp PCC 6803. J. Biol. Chem. 283, 22390-22399. doi: 10. 1074/jbc. M801917200
    • (2008) J. Biol. Chem , vol.283 , pp. 22390-22399
    • Komenda, J.1    Nickelsen, J.2    Tichý, M.3    Prášil, O.4    Eichacker, L.A.5    Nixon, P.J.6
  • 23
    • 10344256210 scopus 로고    scopus 로고
    • Accumulation of the D2 protein is a key regulatory step for assembly of the photosystem II reaction center complex in Synechocystis PCC 6803
    • Komenda, J., Reisinger, V., Müller, B. C., Dobáková, M., Granvogl, B., and Eichacker, L. A. (2004). Accumulation of the D2 protein is a key regulatory step for assembly of the photosystem II reaction center complex in Synechocystis PCC 6803. J. Biol. Chem. 279, 48620-48629. doi: 10. 1074/jbc. M405725200
    • (2004) J. Biol. Chem , vol.279 , pp. 48620-48629
    • Komenda, J.1    Reisinger, V.2    Müller, B.C.3    Dobáková, M.4    Granvogl, B.5    Eichacker, L.A.6
  • 24
    • 84861693795 scopus 로고    scopus 로고
    • Assembling and maintaining the Photosystem II complex in chloroplasts and cyanobacteria
    • Komenda, J., Sobotka, R., and Nixon, P. J. (2012). Assembling and maintaining the Photosystem II complex in chloroplasts and cyanobacteria. Curr. Opin. Plant Biol. 15, 245-251. doi: 10. 1016/j. pbi. 2012. 01. 017
    • (2012) Curr. Opin. Plant Biol , vol.15 , pp. 245-251
    • Komenda, J.1    Sobotka, R.2    Nixon, P.J.3
  • 25
    • 84942905238 scopus 로고    scopus 로고
    • Lack of phosphatidylglycerol inhibits chlorophyll biosynthesis at multiple sites and limits chlorophyllide reutilization in Synechocystis sp. Strain PCC 6803
    • Kopečná, J., Pilný, J., Krynická, V., Tomèala, A., Kis, M., Gombos, Z., et al. (2015). Lack of phosphatidylglycerol inhibits chlorophyll biosynthesis at multiple sites and limits chlorophyllide reutilization in Synechocystis sp. Strain PCC 6803. Plant Physiol. 169, 1307-1317. doi: 10. 1104/pp. 15. 01150
    • (2015) Plant Physiol , vol.169 , pp. 1307-1317
    • Kopečná, J.1    Pilný, J.2    Krynická, V.3    Tomèala, A.4    Kis, M.5    Gombos, Z.6
  • 26
    • 84873086945 scopus 로고    scopus 로고
    • Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem I and Photosystem II in the cyanobacterium Synechocystis PCC 6803
    • Kopečná, J., Sobotka, R., and Komenda, J. (2013). Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem I and Photosystem II in the cyanobacterium Synechocystis PCC 6803. Planta 237, 497-508. doi: 10. 1007/s00425-012-1761-4
    • (2013) Planta , vol.237 , pp. 497-508
    • Kopečná, J.1    Sobotka, R.2    Komenda, J.3
  • 27
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity
    • Kurisu, G., Zhang, H. M., Smith, J. L., and Cramer, W. A. (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302, 1009-1014. doi: 10. 1126/science. 1090165
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.M.2    Smith, J.L.3    Cramer, W.A.4
  • 28
    • 41449093999 scopus 로고    scopus 로고
    • Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacteriumSynechocystis sp PCC 6803
    • Minamizaki, K., Mizoguchi, T., Goto, T., Tamiaki, H., and Fujita, Y. (2008). Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacteriumSynechocystis sp PCC 6803. J. Biol. Chem. 283, 2684-2692. doi: 10. 1074/jbc. M708954200
    • (2008) J. Biol. Chem , vol.283 , pp. 2684-2692
    • Minamizaki, K.1    Mizoguchi, T.2    Goto, T.3    Tamiaki, H.4    Fujita, Y.5
  • 30
    • 0038025174 scopus 로고    scopus 로고
    • Assembly of the D1 precursor in monomeric photosystem II reaction center precomplexes precedes chlorophyll a-triggered accumulation of reaction center II in barley etioplasts
    • Müller, B., and Eichacker, L. A. (1999). Assembly of the D1 precursor in monomeric photosystem II reaction center precomplexes precedes chlorophyll a-triggered accumulation of reaction center II in barley etioplasts. Plant Cell 11, 2365-2377. doi: 10. 2307/3870961
    • (1999) Plant Cell , vol.11 , pp. 2365-2377
    • Müller, B.1    Eichacker, L.A.2
  • 31
    • 0025284693 scopus 로고
    • Chlorophyll regulates accumulation of the plastid encoded chlorophyll apoprotein CP43 and apoprotein D1 by increasing apoprotein stability
    • Mullet, J. E., Klein, P. G., and Klein, R. R. (1990). Chlorophyll regulates accumulation of the plastid encoded chlorophyll apoprotein CP43 and apoprotein D1 by increasing apoprotein stability. Proc. Natl. Acad. Sci. U. S. A. 87, 4038-4042. doi: 10. 1073/pnas. 87. 11. 4038
    • (1990) Proc. Natl. Acad. Sci. U. S. A , vol.87 , pp. 4038-4042
    • Mullet, J.E.1    Klein, P.G.2    Klein, R.R.3
  • 32
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • Nixon, P. J., Michoux, F., Yu, J., Boehm, M., and Komenda, J. (2010). Recent advances in understanding the assembly and repair of photosystem II. Ann. Bot. 106, 1-16. doi: 10. 1093/aob/mcq059
    • (2010) Ann. Bot , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.3    Boehm, M.4    Komenda, J.5
  • 33
    • 69449103993 scopus 로고    scopus 로고
    • Differential requirement of two homologous proteins encoded by sll1214 and sll1874 for the reaction of Mg protoporphyrin monomethylester oxidative cyclase under aerobic and micro-oxic growth conditions
    • Peter, E., Salinas, A., Wallner, T., Jeske, D., Dienst, D., Wilde, A., et al. (2009). Differential requirement of two homologous proteins encoded by sll1214 and sll1874 for the reaction of Mg protoporphyrin monomethylester oxidative cyclase under aerobic and micro-oxic growth conditions. Biochim. Biophys. Acta 1787, 1458-1467. doi: 10. 1016/j. bbabio. 2009. 06. 006
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1458-1467
    • Peter, E.1    Salinas, A.2    Wallner, T.3    Jeske, D.4    Dienst, D.5    Wilde, A.6
  • 34
    • 0036178443 scopus 로고    scopus 로고
    • Rubrivivax gelatinosusacsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester
    • Pinta, V., Picaud, M., Reiss-Husson, F., and Astier, C. (2002). Rubrivivax gelatinosusacsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J. Bacteriol. 184, 746-753. doi: 10. 1128/JB. 184. 3. 746-753. 2002
    • (2002) J. Bacteriol , vol.184 , pp. 746-753
    • Pinta, V.1    Picaud, M.2    Reiss-Husson, F.3    Astier, C.4
  • 35
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simulataneous 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., Thompson, W., and Kriedemann, P. (1989). Determination of accurate extinction coefficients and simulataneous 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, 384-389. doi: 10. 1016/S0005-2728(89)80347-0
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-389
    • Porra, R.1    Thompson, W.2    Kriedemann, P.3
  • 36
    • 0029899561 scopus 로고    scopus 로고
    • Origin of the two carbonyl oxygens of bacteriochlorophyll alpha-Demonstration of two different pathways for the formation of ring E in Rhodobacter sphaeroides andRoseobacter denitrificans, and a common hydratase mechanism for 3-acetyl group formation
    • Porra, R. J., Schafer, W., Gadon, N., Katheder, I., Drews, G., and Scheer, H. (1996). Origin of the two carbonyl oxygens of bacteriochlorophyll alpha-Demonstration of two different pathways for the formation of ring E in Rhodobacter sphaeroides andRoseobacter denitrificans, and a common hydratase mechanism for 3-acetyl group formation. Eur. J. Biochem. 239, 85-92. doi: 10. 1111/j. 1432-1033. 1996. 0085u. x
    • (1996) Eur. J. Biochem , vol.239 , pp. 85-92
    • Porra, R.J.1    Schafer, W.2    Gadon, N.3    Katheder, I.4    Drews, G.5    Scheer, H.6
  • 37
    • 33845926012 scopus 로고    scopus 로고
    • Cyanobacterial small chlorophyll-binding protein ScpD (HliB) is located on the periphery of photosystem II in the vicinity of PsbH and CP47 subunits
    • Promnares, K., Komenda, J., Bumba, L., Nebesarova, J., Vacha, F., and Tichy, M. (2006). Cyanobacterial small chlorophyll-binding protein ScpD (HliB) is located on the periphery of photosystem II in the vicinity of PsbH and CP47 subunits. J. Biol. Chem. 281, 32705-32713. doi: 10. 1074/jbc. M606360200
    • (2006) J. Biol. Chem , vol.281 , pp. 32705-32713
    • Promnares, K.1    Komenda, J.2    Bumba, L.3    Nebesarova, J.4    Vacha, F.5    Tichy, M.6
  • 38
    • 0016671050 scopus 로고
    • Chloroplast biogenesis. Biosynthesis and accumulation of Mg-protoprophyrin IX monoester and longer wavelength metalloporphyrins by greening cotyledons
    • Rebeiz, C. A., Mattheis, J. R., Smith, B. B., Rebeiz, C., and Dayton, D. F. (1975). Chloroplast biogenesis. Biosynthesis and accumulation of Mg-protoprophyrin IX monoester and longer wavelength metalloporphyrins by greening cotyledons. Arch. Biochem. Biophys. 166, 446-465. doi: 10. 1016/0003-9861(75)90408-7
    • (1975) Arch. Biochem. Biophys , vol.166 , pp. 446-465
    • Rebeiz, C.A.1    Mattheis, J.R.2    Smith, B.B.3    Rebeiz, C.4    Dayton, D.F.5
  • 39
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., Deruelles, J., Waterbury, J., Herdman, M., and Stanier, R. (1979). Generic assignments, strain histories and properties of pure cultures of cyanobacteria. Microbiology 111, 1-61. doi: 10. 1099/00221287-111-1-1
    • (1979) Microbiology , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.3    Herdman, M.4    Stanier, R.5
  • 40
    • 54449102004 scopus 로고    scopus 로고
    • Importance of the cyanobacterial GUN4 protein for chlorophyll metabolism and assembly of photosynthetic complexes
    • Sobotka, R., Duerhring, U., Komenda, J., Peter, E., Gardian, Z., Tichy, M., et al. (2008). Importance of the cyanobacterial GUN4 protein for chlorophyll metabolism and assembly of photosynthetic complexes. J. Biol. Chem. 283, 25794-25802. doi: 10. 1074/jbc. M803787200
    • (2008) J. Biol. Chem , vol.283 , pp. 25794-25802
    • Sobotka, R.1    Duerhring, U.2    Komenda, J.3    Peter, E.4    Gardian, Z.5    Tichy, M.6
  • 41
    • 79953712614 scopus 로고    scopus 로고
    • Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis
    • Sobotka, R., Tichy, M., Wilde, A., and Hunter, C. N. (2011). Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: the CAB domain plays a regulatory role, and region II is essential for catalysis. Plant Physiol. 155, 1735-1747. doi: 10. 1104/pp. 110. 167528
    • (2011) Plant Physiol , vol.155 , pp. 1735-1747
    • Sobotka, R.1    Tichy, M.2    Wilde, A.3    Hunter, C.N.4
  • 42
    • 84925860495 scopus 로고    scopus 로고
    • Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins
    • Staleva, H., Komenda, J., Shukla, M. K., Šlouf, V., Kaòa, R., Polívka, T., et al. (2015). Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins. Nat. Chem. Biol. 11, 287-291. doi: 10. 1038/nchembio. 1755
    • (2015) Nat. Chem. Biol , vol.11 , pp. 287-291
    • Staleva, H.1    Komenda, J.2    Shukla, M.K.3    Šlouf, V.4    Kaòa, R.5    Polívka, T.6
  • 43
    • 0000445956 scopus 로고
    • Excitation sculpting in high-resolution nuclear magnetic resonance spectroscopy: Application to selective NOE experiments
    • Stott, K., Stonehouse, J., Keeler, J., Hwang, T., and Shaka, A. (1995). Excitation sculpting in high-resolution nuclear magnetic resonance spectroscopy: application to selective NOE experiments. J. Am. Chem. Soc. 117, 4199-4200. doi: 10. 1021/ja00119a048
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 4199-4200
    • Stott, K.1    Stonehouse, J.2    Keeler, J.3    Hwang, T.4    Shaka, A.5
  • 44
    • 41149116094 scopus 로고    scopus 로고
    • Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina
    • Swingley, W. D., Chen, M., Cheung, P. C., Conrad, A. L., Dejesa, L. C., Hao, J., et al. (2008). Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina. Proc. Natl. Acad. Sci. U. S. A. 105, 2005-2010. doi: 10. 1073/pnas. 0709772105
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 2005-2010
    • Swingley, W.D.1    Chen, M.2    Cheung, P.C.3    Conrad, A.L.4    Dejesa, L.C.5    Hao, J.6
  • 45
    • 0347364625 scopus 로고    scopus 로고
    • Arabidopsis CHL27, located in both envelope and thylakoid membranes, is required for the synthesis of protochlorophyllide
    • Tottey, S., Block, M. A., Allen, M., Westergren, T., Albrieux, C., Scheller, H. V., et al. (2003). Arabidopsis CHL27, located in both envelope and thylakoid membranes, is required for the synthesis of protochlorophyllide. Proc. Natl. Acad. Sci. U. S. A. 100, 16119-16124. doi: 10. 1073/pnas. 2136793100
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 16119-16124
    • Tottey, S.1    Block, M.A.2    Allen, M.3    Westergren, T.4    Albrieux, C.5    Scheller, H.V.6
  • 46
    • 84870851200 scopus 로고    scopus 로고
    • Microevolution in cyanobacteria: Re-sequencing a motile substrain of Synechocystis sp. PCC 6803
    • Trautmann, D., Voss, B., Wilde, A., Al-Babili, S., and Hess, W. R. (2012). Microevolution in cyanobacteria: re-sequencing a motile substrain of Synechocystis sp. PCC 6803. DNA Res. 19, 435-448. doi: 10. 1093/dnares/dss024
    • (2012) DNA Res , vol.19 , pp. 435-448
    • Trautmann, D.1    Voss, B.2    Wilde, A.3    Al-Babili, S.4    Hess, W.R.5
  • 47
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1. 9 Å
    • Umena, Y., Kawakami, K., Shen, J. R., and Kamiya, N. (2011). Crystal structure of oxygen-evolving photosystem II at a resolution of 1. 9 Å. Nature 473, 55-60. doi: 10. 1038/nature09913
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 48
    • 29144514372 scopus 로고    scopus 로고
    • The three-dimensional structure of the cyanobacterium Synechocystis sp. PCC 6803
    • van de Meene, A. M., Hohmann-Marriott, M. F., Vermaas, W. F., and Roberson, R. W. (2006). The three-dimensional structure of the cyanobacterium Synechocystis sp. PCC 6803. Arch. Microbiol. 184, 259-270.
    • (2006) Arch. Microbiol , vol.184 , pp. 259-270
    • van de Meene, A.M.1    Hohmann-Marriott, M.F.2    Vermaas, W.F.3    Roberson, R.W.4
  • 49
    • 34447092491 scopus 로고    scopus 로고
    • Continuous chlorophyll degradation accompanied by chlorophyllide and phytol reutilization for chlorophyll synthesis in Synechocystis sp PCC 6803
    • Vavilin, D., and Vermaas, W. (2007). Continuous chlorophyll degradation accompanied by chlorophyllide and phytol reutilization for chlorophyll synthesis in Synechocystis sp PCC 6803. Biochim. Biophys. Acta 1767, 920-929. doi: 10. 1016/j. bbabio. 2007. 03. 010
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 920-929
    • Vavilin, D.1    Vermaas, W.2
  • 50
    • 3342976152 scopus 로고    scopus 로고
    • The gun4 gene is essential for cyanobacterial porphyrin metabolism
    • Wilde, A., Mikolajczyk, S., Alawady, A., Lokstein, H., and Grimm, B. (2004). The gun4 gene is essential for cyanobacterial porphyrin metabolism. FEBS Lett. 571, 119-123. doi: 10. 1016/j. febslet. 2004. 06. 063
    • (2004) FEBS Lett , vol.571 , pp. 119-123
    • Wilde, A.1    Mikolajczyk, S.2    Alawady, A.3    Lokstein, H.4    Grimm, B.5
  • 51
    • 84951150566 scopus 로고    scopus 로고
    • Isotope-encoded carboxyl group footprinting for mass spectrometry-based protein conformational studies
    • Zhang, H., Liu, H., Blankenship, R. E., and Gross, M. L. (2015). Isotope-encoded carboxyl group footprinting for mass spectrometry-based protein conformational studies. J. Am. Soc. Mass Spectrom. 27, 178-181. doi: 10. 1007/s13361-015-1260-5
    • (2015) J. Am. Soc. Mass Spectrom , vol.27 , pp. 178-181
    • Zhang, H.1    Liu, H.2    Blankenship, R.E.3    Gross, M.L.4
  • 52
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3. 8 Å resolution
    • Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W., et al. (2001). Crystal structure of photosystem II from Synechococcus elongatus at 3. 8 Å resolution. Nature 409, 739-743. doi: 10. 1038/35055589
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.