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Volumn 119, Issue 1-2, 2014, Pages 223-232

Making proteins green; Biosynthesis of chlorophyll-binding proteins in cyanobacteria

Author keywords

Chlorophyll biosynthesis; Chlorophyll binding proteins; Cofactors; Cyanobacteria; Tetrapyrroles

Indexed keywords

CYANOBACTERIA;

EID: 84891633185     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-013-9797-2     Document Type: Review
Times cited : (54)

References (80)
  • 1
    • 79957672967 scopus 로고    scopus 로고
    • GUN4-porphyrin complexes bind the ChlH/GUN5 subunit of Mg-chelatase and promote chlorophyll biosynthesis in Arabidopsis
    • 1:CAS:528:DC%2BC3MXnsl2lurg%3D 3101535 21467578 10.1105/tpc.110.082503
    • Adhikari ND, Froehlich JE, Strand DD, Buck SM, Kramer DM, Larkin RM (2011) GUN4-porphyrin complexes bind the ChlH/GUN5 subunit of Mg-chelatase and promote chlorophyll biosynthesis in Arabidopsis. Plant Cell 23:1449-1467
    • (2011) Plant Cell , vol.23 , pp. 1449-1467
    • Adhikari, N.D.1    Froehlich, J.E.2    Strand, D.D.3    Buck, S.M.4    Kramer, D.M.5    Larkin, R.M.6
  • 2
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress, and signal transduction
    • 1:CAS:528:DC%2BD2cXlvFeisL0%3D 15377225 10.1146/annurev.arplant.55. 031903.141701
    • Apel K, Hirt H (2004) Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55:373-399
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 3
    • 57549094142 scopus 로고    scopus 로고
    • Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis
    • 1:CAS:528:DC%2BD1MXlsV2ltg%3D%3D 18764927 10.1111/j.1365-313X.2008.03659. x
    • Asakura Y, Kikuchi S, Nakai M (2008) Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis. Plant J 56:1007-1017
    • (2008) Plant J , vol.56 , pp. 1007-1017
    • Asakura, Y.1    Kikuchi, S.2    Nakai, M.3
  • 4
    • 84862765893 scopus 로고    scopus 로고
    • Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells
    • 1:CAS:528:DC%2BC38XhtFegtL3K 3383343 22624875 10.1111/j.1365-2958.2012. 08081.x
    • Bakshi S, Siryaporn A, Goulian M, Weisshaar JC (2012) Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells. Mol Microbiol 85:21-38
    • (2012) Mol Microbiol , vol.85 , pp. 21-38
    • Bakshi, S.1    Siryaporn, A.2    Goulian, M.3    Weisshaar, J.C.4
  • 5
    • 0017171618 scopus 로고
    • Periodic variations in the ratio of free to thylakoid-bound chloroplast ribosomes during the cell cycle of Chlamydomonas reinhardtii
    • 1:CAS:528:DyaE28XlvV2nsLg%3D 993261 10.1083/jcb.71.2.497
    • Chua NH, Blobel G, Siekevitz P, Palade GE (1976) Periodic variations in the ratio of free to thylakoid-bound chloroplast ribosomes during the cell cycle of Chlamydomonas reinhardtii. J Cell Biol 71:497-514
    • (1976) J Cell Biol , vol.71 , pp. 497-514
    • Chua, N.H.1    Blobel, G.2    Siekevitz, P.3    Palade, G.E.4
  • 6
    • 84857983500 scopus 로고    scopus 로고
    • Post-translational control of tetrapyrrole biosynthesis in plants, algae, and cyanobacteria
    • 1:CAS:528:DC%2BC38XjtlKhsbs%3D 22231500 10.1093/jxb/err437
    • Czarnecki O, Grimm B (2012) Post-translational control of tetrapyrrole biosynthesis in plants, algae, and cyanobacteria. J Exp Bot 63:1675-1687
    • (2012) J Exp Bot , vol.63 , pp. 1675-1687
    • Czarnecki, O.1    Grimm, B.2
  • 7
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • 1:CAS:528:DC%2BC3MXptVCns7s%3D 21275640 10.1146/annurev-biochem-060409- 092524
    • Dalbey RE, Wang P, Kuhn A (2011) Assembly of bacterial inner membrane proteins. Annu Rev Biochem 80:161-187
    • (2011) Annu Rev Biochem , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 8
    • 19644396905 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis
    • 1:CAS:528:DC%2BD2MXjslKlsrY%3D 15909975 10.1021/bi050240x
    • Davison PA, Schubert HL, Reid JD, Iorg CD, Heroux A, Hill CP, Hunter CN (2005) Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis. Biochemistry 44:7603-7612
    • (2005) Biochemistry , vol.44 , pp. 7603-7612
    • Davison, P.A.1    Schubert, H.L.2    Reid, J.D.3    Iorg, C.D.4    Heroux, A.5    Hill, C.P.6    Hunter, C.N.7
  • 9
    • 0028843343 scopus 로고
    • Cyanobacterial protein with similarity to the chlorophyll a/b binding proteins of higher plants: Evolution and regulation
    • 1:CAS:528:DyaK2MXjt12qtbg%3D 7831342 10.1073/pnas.92.2.636
    • Dolganov NA, Bhaya D, Grossman AR (1995) Cyanobacterial protein with similarity to the chlorophyll a/b binding proteins of higher plants: evolution and regulation. Proc Natl Acad Sci USA 92:636-640
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 636-640
    • Dolganov, N.A.1    Bhaya, D.2    Grossman, A.R.3
  • 10
    • 0038175113 scopus 로고    scopus 로고
    • Characterization of two phases of chlorophyll formation during greening of etiolated barley leaves
    • 1:CAS:528:DC%2BD3sXhtlOitb0%3D 12520340
    • Domanskii V, Rassadina V, Gus-Mayer S, Wanner G, Schoch S, Rudiger W (2003) Characterization of two phases of chlorophyll formation during greening of etiolated barley leaves. Planta 216:475-483
    • (2003) Planta , vol.216 , pp. 475-483
    • Domanskii, V.1    Rassadina, V.2    Gus-Mayer, S.3    Wanner, G.4    Schoch, S.5    Rudiger, W.6
  • 11
    • 80053430265 scopus 로고    scopus 로고
    • Interaction studies between the chloroplast signal recognition particle subunit cpSRP43 and the full-length translocase Alb3 reveal a membrane-embedded binding region in Alb3 protein
    • 21832051 10.1074/jbc.M111.250746
    • Dünschede B, Bals T, Funke S, Schünemann D (2011) Interaction studies between the chloroplast signal recognition particle subunit cpSRP43 and the full-length translocase Alb3 reveal a membrane-embedded binding region in Alb3 protein. J Biol Chem 286:35187-35195
    • (2011) J Biol Chem , vol.286 , pp. 35187-35195
    • Dünschede, B.1    Bals, T.2    Funke, S.3    Schünemann, D.4
  • 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
    • 1:CAS:528:DyaK2sXit1Shtw%3D%3D 8943272 10.1074/jbc.271.50.32174
    • Eichacker LA, Helfrich M, Rüdiger W, Müller 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
    • (1996) J Biol Chem , vol.271 , pp. 32174-32179
    • Eichacker, L.A.1    Helfrich, M.2    Rüdiger, W.3    Müller, B.4
  • 13
    • 0001579901 scopus 로고
    • Regulation of the stoichiometry of thylakoid components in the photosynthetic system of cyanophytes: Model experiments showing that control of the synthesis or supply of Chl a can change the stoichiometric relationship between the two photosystems
    • 1:CAS:528:DyaK3cXhsFGnsLs%3D
    • Fujita Y, Murakami A, Ohki K (1990) Regulation of the stoichiometry of thylakoid components in the photosynthetic system of cyanophytes: model experiments showing that control of the synthesis or supply of Chl a can change the stoichiometric relationship between the two photosystems. Plant Cell Physiol 31:145-153
    • (1990) Plant Cell Physiol , vol.31 , pp. 145-153
    • Fujita, Y.1    Murakami, A.2    Ohki, K.3
  • 14
    • 33745438296 scopus 로고    scopus 로고
    • One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas
    • 10.1105/tpc.105.038695
    • Göhre V, Ossenbühl F, Crèvecoeur M, Eichacker LA, Rochaix JD (2006) One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas. Plant Cell 8:1454-1466
    • (2006) Plant Cell , vol.8 , pp. 1454-1466
    • Göhre, V.1    Ossenbühl, F.2    Crèvecoeur, M.3    Eichacker, L.A.4    Rochaix, J.D.5
  • 15
    • 0023187026 scopus 로고
    • An aminoacyl-tRNA synthetase complex in Escherichia coli
    • 1:CAS:528:DyaL2sXkvFantLw%3D 212173 3294804
    • Harris CL (1987) An aminoacyl-tRNA synthetase complex in Escherichia coli. J Bacteriol 169:2718-2723
    • (1987) J Bacteriol , vol.169 , pp. 2718-2723
    • Harris, C.L.1
  • 16
    • 0033518234 scopus 로고    scopus 로고
    • From molecular to modular cell biology
    • 1:CAS:528:DyaK1MXnslKms70%3D 10591225 10.1038/35011540
    • Hartwell LH, Hopfield JJ, Leibler S, Murray AW (1999) From molecular to modular cell biology. Nature 402(Suppl):C47-C52
    • (1999) Nature , vol.402 , Issue.SUPPL.
    • Hartwell, L.H.1    Hopfield, J.J.2    Leibler, S.3    Murray, A.W.4
  • 17
    • 79960563606 scopus 로고    scopus 로고
    • The small CAB-like proteins of the cyanobacterium Synechocystis sp. PCC 6803: Their involvement in chlorophyll biogenesis for photosystem II
    • 1:CAS:528:DC%2BC3MXptVyqu7g%3D 21605542 10.1016/j.bbabio.2011.05.002
    • Hernandez-Prieto MA, Tibiletti T, Abasova L, Kirilovsky D, Funk C (2011) The small CAB-like proteins of the cyanobacterium Synechocystis sp. PCC 6803: their involvement in chlorophyll biogenesis for photosystem II. Biochim Biophys Acta 1807:1143-1151
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 1143-1151
    • Hernandez-Prieto, M.A.1    Tibiletti, T.2    Abasova, L.3    Kirilovsky, D.4    Funk, C.5
  • 18
    • 0032135117 scopus 로고    scopus 로고
    • A novel gene, pmgA, specifically regulates photosystem stoichiometry in the cyanobacterium Synechocystis species PCC 6803 in response to high light
    • 1:CAS:528:DyaK1cXlsFaqtrs%3D 34885 9701577 10.1104/pp.117.4.1205
    • Hihara Y, Sonoike K, Ikeuchi M (1998) A novel gene, pmgA, specifically regulates photosystem stoichiometry in the cyanobacterium Synechocystis species PCC 6803 in response to high light. Plant Physiol 117:1205-1216
    • (1998) Plant Physiol , vol.117 , pp. 1205-1216
    • Hihara, Y.1    Sonoike, K.2    Ikeuchi, M.3
  • 19
    • 84865015496 scopus 로고    scopus 로고
    • Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase in Synechocystis PCC 6803
    • 1:CAS:528:DC%2BC38XhtFOksb3J 22711541 10.1074/jbc.M112.352526
    • Hollingshead S, Kopečná J, Jackson PJ, Canniffe DP, Davison PA, Dickman MJ, Sobotka R, Hunter CN (2012) Conserved chloroplast open-reading frame ycf54 is required for activity of the magnesium protoporphyrin monomethylester oxidative cyclase in Synechocystis PCC 6803. J Biol Chem 287:27823-27833
    • (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    Sobotka, R.7    Hunter, C.N.8
  • 20
    • 0026499562 scopus 로고
    • Complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid in Chlamydomonas reinhardtii
    • 1:CAS:528:DyaK3sXjsFKgtQ%3D%3D 1451806 10.1016/0014-5793(92)81465-X
    • Jahn D (1992) Complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid in Chlamydomonas reinhardtii. FEBS Lett 314:77-80
    • (1992) FEBS Lett , vol.314 , pp. 77-80
    • Jahn, D.1
  • 22
    • 24044489621 scopus 로고    scopus 로고
    • A previously found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of plant photosystem i and is designated PSI-P
    • 1:CAS:528:DC%2BD2MXpt1ertbY%3D 16109415 10.1016/j.febslet.2005.07.061
    • Khrouchtchova A, Hansson M, Paakkarinen V, Vainonen JP, Zhang S, Jensen PE, Scheller HV, Vener AV, Aro EM, Haldrup A (2005) A previously found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of plant photosystem I and is designated PSI-P. FEBS Lett 579:4808-4812
    • (2005) FEBS Lett , vol.579 , pp. 4808-4812
    • Khrouchtchova, A.1    Hansson, M.2    Paakkarinen, V.3    Vainonen, J.P.4    Zhang, S.5    Jensen, P.E.6    Scheller, H.V.7    Vener, A.V.8    Aro, E.M.9    Haldrup, A.10
  • 23
    • 0028180461 scopus 로고
    • Synthesis and turnover of photosystem II reaction center protein D1. Ribosome pausing increases during chloroplast development
    • 1:CAS:528:DyaK2cXkslymu7k%3D 8027048
    • Kim J, Klein PG, Mullet JE (1994) Synthesis and turnover of photosystem II reaction center protein D1. Ribosome pausing increases during chloroplast development. J Biol Chem 269:17918-17923
    • (1994) J Biol Chem , vol.269 , pp. 17918-17923
    • Kim, J.1    Klein, P.G.2    Mullet, J.E.3
  • 24
    • 0037115768 scopus 로고    scopus 로고
    • The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
    • 1:CAS:528:DC%2BD38XptlyktL4%3D 12217076 10.1042/BJ20021291
    • Klostermann E, Droste Gen Helling I, Carde JP, Schünemann D (2002) The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana. Biochem J 368:777-781
    • (2002) Biochem J , vol.368 , pp. 777-781
    • Klostermann, E.1    Droste Gen Helling, I.2    Carde, J.P.3    Schünemann, D.4
  • 26
    • 0028867489 scopus 로고
    • Functional and structural changes of the photosystem II complex induced by high irradiance in cyanobacterial cells
    • 1:CAS:528:DyaK2MXptlKqs7k%3D 7588816 10.1111/j.1432-1033.1995.677-2.x
    • Komenda J, Masojídek J (1995) Functional and structural changes of the photosystem II complex induced by high irradiance in cyanobacterial cells. Eur J Biochem 233:677-682
    • (1995) Eur J Biochem , vol.233 , pp. 677-682
    • Komenda, J.1    Masojídek, J.2
  • 27
    • 84861693795 scopus 로고    scopus 로고
    • Assembling and maintaining the photosystem II complex in chloroplasts and cyanobacteria
    • 1:CAS:528:DC%2BC38Xnsl2qsbo%3D 22386092 10.1016/j.pbi.2012.01.017
    • Komenda J, Sobotka R, Nixon PJ (2012) Assembling and maintaining the photosystem II complex in chloroplasts and cyanobacteria. Curr Opin Plant Biol 15:245-251
    • (2012) Curr Opin Plant Biol , vol.15 , pp. 245-251
    • Komenda, J.1    Sobotka, R.2    Nixon, P.J.3
  • 28
    • 84870788945 scopus 로고    scopus 로고
    • Long-term acclimation of the cyanobacterium Synechocystis PCC 6803 to high light is accompanied by an enhanced production of chlorophyll that is preferentially channeled to trimeric PSI
    • 3510144 23037506 10.1104/pp.112.207274
    • Kopečná J, Komenda J, Bučinská L, Sobotka R (2012) Long-term acclimation of the cyanobacterium Synechocystis PCC 6803 to high light is accompanied by an enhanced production of chlorophyll that is preferentially channeled to trimeric PSI. Plant Physiol 160:2239-2250
    • (2012) Plant Physiol , vol.160 , pp. 2239-2250
    • Kopečná, J.1    Komenda, J.2    Bučinská, L.3    Sobotka, R.4
  • 29
    • 84873086945 scopus 로고    scopus 로고
    • Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletionof photosystem i and photosystem II in the cyanobacterium Synechocystis PCC 6803
    • Kopečná J, Sobotka R, Komenda J (2013) Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletionof photosystem I and photosystem II in the cyanobacterium Synechocystis PCC 6803. Planta 237:497-508
    • (2013) Planta , vol.237 , pp. 497-508
    • Kopečná, J.1    Sobotka, R.2    Komenda, J.3
  • 30
    • 39549104965 scopus 로고    scopus 로고
    • An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth
    • 1:CAS:528:DC%2BD1cXjtFCgsbg%3D 2273998 18313381 10.1016/j.molcel.2007.11. 038
    • Kyriacou SV, Deutscher MP (2008) An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth. Mol Cell 29:419-427
    • (2008) Mol Cell , vol.29 , pp. 419-427
    • Kyriacou, S.V.1    Deutscher, M.P.2
  • 31
    • 0347298576 scopus 로고    scopus 로고
    • GUN4, a regulator of chlorophyll synthesis and intracellular signaling
    • 1:CAS:528:DC%2BD3sXpt1SgsQ%3D%3D 12574634 10.1126/science.1079978
    • Larkin RM, Alonso JM, Ecker JR, Chory J (2003) GUN4, a regulator of chlorophyll synthesis and intracellular signaling. Science 299:902-906
    • (2003) Science , vol.299 , pp. 902-906
    • Larkin, R.M.1    Alonso, J.M.2    Ecker, J.R.3    Chory, J.4
  • 32
    • 21444433241 scopus 로고    scopus 로고
    • Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis
    • 15757895 10.1074/jbc.M500440200
    • Lüer C, Schauer S, Möbius K, Schulze J, Schubert WD, Heinz DW, Jahn D, Moser J (2005) Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis. J Biol Chem 280:18568-18572
    • (2005) J Biol Chem , vol.280 , pp. 18568-18572
    • Lüer, C.1    Schauer, S.2    Möbius, K.3    Schulze, J.4    Schubert, W.D.5    Heinz, D.W.6    Jahn, D.7    Moser, J.8
  • 33
    • 84860551566 scopus 로고    scopus 로고
    • Thioredoxin redox regulates ATPase activity of magnesium chelatase CHLI subunit and modulates redox-mediated signaling in tetrapyrrole biosynthesis and homeostasis of reactive oxygen species in pea plants
    • 1:CAS:528:DC%2BC38XntV2gsr0%3D 3375955 22452855 10.1104/pp.112.195446
    • Luo T, Fan T, Liu Y, Rothbart M, Yu J, Zhou S, Grimm B, Luo M (2012) Thioredoxin redox regulates ATPase activity of magnesium chelatase CHLI subunit and modulates redox-mediated signaling in tetrapyrrole biosynthesis and homeostasis of reactive oxygen species in pea plants. Plant Physiol 159:118-130
    • (2012) Plant Physiol , vol.159 , pp. 118-130
    • Luo, T.1    Fan, T.2    Liu, Y.3    Rothbart, M.4    Yu, J.5    Zhou, S.6    Grimm, B.7    Luo, M.8
  • 34
    • 58949086104 scopus 로고    scopus 로고
    • Complex formation between protoporphyrinogen IX oxidase and ferrochelatase during haem biosynthesis in Thermosynechococcus elongatus
    • 1:CAS:528:DC%2BD1MXhsVCjuw%3D%3D 19047738 10.1099/mic.0.2008/018705-0
    • Masoumi A, Heinemann IU, Rohde M, Koch M, Jahn M, Jahn D (2008) Complex formation between protoporphyrinogen IX oxidase and ferrochelatase during haem biosynthesis in Thermosynechococcus elongatus. Microbiology 154:3707-3714
    • (2008) Microbiology , vol.154 , pp. 3707-3714
    • Masoumi, A.1    Heinemann, I.U.2    Rohde, M.3    Koch, M.4    Jahn, M.5    Jahn, D.6
  • 35
    • 53749102865 scopus 로고    scopus 로고
    • Regulation and evolution of chlorophyll metabolism
    • 10.1039/b807210h
    • Masuda T, Fujita Y (2008) Regulation and evolution of chlorophyll metabolism. Photochem Photobiol Sci 10:1131-1149
    • (2008) Photochem Photobiol Sci , vol.10 , pp. 1131-1149
    • Masuda, T.1    Fujita, Y.2
  • 36
    • 0141530036 scopus 로고    scopus 로고
    • Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: Substrate not required
    • 1:CAS:528:DC%2BD3sXnsl2jsb4%3D 14517205 10.1083/jcb.200307067
    • Moore M, Goforth RL, Mori H, Henry R (2003) Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required. J Cell Biol 162:1245-1254
    • (2003) J Cell Biol , vol.162 , pp. 1245-1254
    • Moore, M.1    Goforth, R.L.2    Mori, H.3    Henry, R.4
  • 37
    • 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
    • 144137 10590164
    • Müller B, Eichacker LA (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
    • (1999) Plant Cell , vol.11 , pp. 2365-2377
    • Müller, B.1    Eichacker, L.A.2
  • 38
    • 0025284693 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability
    • 1:CAS:528:DyaK3cXkslGis7Y%3D 2349216 10.1073/pnas.87.11.4038
    • Mullet JE, Klein PG, Klein RR (1990) Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability. Proc Natl Acad Sci USA 87:4038-4042
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4038-4042
    • Mullet, J.E.1    Klein, P.G.2    Klein, R.R.3
  • 39
    • 64049097710 scopus 로고    scopus 로고
    • Mechanism of downregulation of photosystem i content under high-light conditions in the cyanobacterium synechocystis sp. PCC 6803
    • 1:CAS:528:DC%2BD1MXjs1Wkt74%3D 19246769 10.1099/mic.0.024018-0
    • Muramatsu M, Sonoike K, Hihara Y (2009) Mechanism of downregulation of photosystem I content under high-light conditions in the cyanobacterium synechocystis sp. PCC 6803. Microbiology 155:989-996
    • (2009) Microbiology , vol.155 , pp. 989-996
    • Muramatsu, M.1    Sonoike, K.2    Hihara, Y.3
  • 40
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • 1:CAS:528:DC%2BD2cXjtFGqu7k%3D 15067017 10.1083/jcb.200402067
    • Nagamori S, Smirnova IN, Kaback HR (2004) Role of YidC in folding of polytopic membrane proteins. J Cell Biol 165:53-62
    • (2004) J Cell Biol , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 41
    • 78650169950 scopus 로고    scopus 로고
    • Structural and functional diversification of the light-harvesting complexes in photosynthetic eukaryotes
    • 1:CAS:528:DC%2BC3cXht1ahtbfI 20596891 10.1007/s11120-010-9576-2
    • Neilson JA, Durnford DG (2010) Structural and functional diversification of the light-harvesting complexes in photosynthetic eukaryotes. Photosyn Res 106:57-71
    • (2010) Photosyn Res , vol.106 , pp. 57-71
    • Neilson, J.A.1    Durnford, D.G.2
  • 42
    • 0037205751 scopus 로고    scopus 로고
    • Transient interaction of cpSRP54 with elongating nascent chains of the chloroplast-encoded D1 protein; 'cpSRP54 caught in the act'
    • 1:CAS:528:DC%2BD38Xls1Wlu7s%3D 12135754 10.1016/S0014-5793(02)03016-8
    • Nilsson R, van Wijk KJ (2002) Transient interaction of cpSRP54 with elongating nascent chains of the chloroplast-encoded D1 protein; 'cpSRP54 caught in the act'. FEBS Lett 524:127-133
    • (2002) FEBS Lett , vol.524 , pp. 127-133
    • Nilsson, R.1    Van Wijk, K.J.2
  • 43
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • 1:CAS:528:DC%2BC3cXotVWjsb4%3D 20338950 10.1093/aob/mcq059
    • Nixon PJ, Michoux F, Yu J, Boehm M, Komenda J (2010) Recent advances in understanding the assembly and repair of photosystem II. Ann Bot 106:1-16
    • (2010) Ann Bot , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.3    Boehm, M.4    Komenda, J.5
  • 44
    • 21644490055 scopus 로고    scopus 로고
    • Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii
    • 1:CAS:528:DC%2BD2MXlsFyrt7c%3D 15890644 10.1074/jbc.M502483200
    • Nogaj LA, Beale SI (2005) Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii. J Biol Chem 280:24301-24307
    • (2005) J Biol Chem , vol.280 , pp. 24301-24307
    • Nogaj, L.A.1    Beale, S.I.2
  • 45
    • 0029165965 scopus 로고
    • Hypothesis: Chromosome separation in Escherichia coli involves autocatalytic gene expression, transertion and membrane-domain formation
    • 1:CAS:528:DyaK2MXntlKgurk%3D 8577241 10.1111/j.1365-2958.1995.tb02330.x
    • Norris V (1995) Hypothesis: chromosome separation in Escherichia coli involves autocatalytic gene expression, transertion and membrane-domain formation. Mol Microbiol 16:1051-1057
    • (1995) Mol Microbiol , vol.16 , pp. 1051-1057
    • Norris, V.1
  • 47
    • 33845746230 scopus 로고    scopus 로고
    • Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of photosystem II
    • 1:CAS:528:DC%2BD2sXit1Cktw%3D%3D 1693947 17114356 10.1105/tpc.106.042671
    • Nowaczyk MM, Hebeler R, Schlodder E, Meyer HE, Warscheid B, Rögner M (2006) Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of photosystem II. Plant Cell 18:3121-3131
    • (2006) Plant Cell , vol.18 , pp. 3121-3131
    • Nowaczyk, M.M.1    Hebeler, R.2    Schlodder, E.3    Meyer, H.E.4    Warscheid, B.5    Rögner, M.6
  • 48
    • 81755172410 scopus 로고    scopus 로고
    • Membrane anchoring of aminoacyl-tRNA synthetases by convergent acquisition of a novel protein domain
    • 1:CAS:528:DC%2BC3MXhsVOqu7fK 21965654 10.1074/jbc.M111.242461
    • Olmedo-Verd E, Santamaría-Gómez J, Ochoa de Alda JA, Ribas de Pouplana L, Luque I (2011) Membrane anchoring of aminoacyl-tRNA synthetases by convergent acquisition of a novel protein domain. J Biol Chem 286:41057-41068
    • (2011) J Biol Chem , vol.286 , pp. 41057-41068
    • Olmedo-Verd, E.1    Santamaría-Gómez, J.2    Ochoa De Alda, J.A.3    Ribas De Pouplana, L.4    Luque, I.5
  • 49
    • 66149094287 scopus 로고    scopus 로고
    • ChlH, the H subunit of the Mg-chelatase, is an anti-sigma factor for SigE in Synechocystis sp. PCC 6803
    • 1:CAS:528:DC%2BD1MXlsFansb4%3D 19342483 10.1073/pnas.0810040106
    • Osanai T, Imashimizu M, Seki A, Sato S, Tabata S, Imamura S, Asayama M, Ikeuchi M, Tanaka K (2009) ChlH, the H subunit of the Mg-chelatase, is an anti-sigma factor for SigE in Synechocystis sp. PCC 6803. Proc Natl Acad Sci USA 106:6860-6865
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6860-6865
    • Osanai, T.1    Imashimizu, M.2    Seki, A.3    Sato, S.4    Tabata, S.5    Imamura, S.6    Asayama, M.7    Ikeuchi, M.8    Tanaka, K.9
  • 50
    • 33749258554 scopus 로고    scopus 로고
    • The Synechocystis sp. PCC 6803 Oxa1 homolog is essential for membrane integration of reaction center precursor protein pD1
    • 1560907 16905652 10.1105/tpc.106.043646
    • Ossenbühl F, Inaba-Sulpice M, Meurer J, Soll J, Eichacker LA (2006) The Synechocystis sp. PCC 6803 Oxa1 homolog is essential for membrane integration of reaction center precursor protein pD1. Plant Cell 18:2236-2246
    • (2006) Plant Cell , vol.18 , pp. 2236-2246
    • Ossenbühl, F.1    Inaba-Sulpice, M.2    Meurer, J.3    Soll, J.4    Eichacker, L.A.5
  • 51
    • 60349086107 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution
    • 1:CAS:528:DC%2BD1MXivFentro%3D 19187240 10.1111/j.1742-4658.2009.06880.x
    • Paravisi S, Fumagalli G, Riva M, Morandi P, Morosi R, Konarev PV, Petoukhov MV, Bernier S, Chênevert R, Svergun DI, Curti B, Vanoni MA (2009) Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution. FEBS J 276:1398-1417
    • (2009) FEBS J , vol.276 , pp. 1398-1417
    • Paravisi, S.1    Fumagalli, G.2    Riva, M.3    Morandi, P.4    Morosi, R.5    Konarev, P.V.6    Petoukhov, M.V.7    Bernier, S.8    Chênevert, R.9    Svergun, D.I.10    Curti, B.11    Vanoni, M.A.12
  • 52
    • 28444458466 scopus 로고    scopus 로고
    • The yeast split-ubiquitin system to study chloroplast membrane protein interactions
    • 1:CAS:528:DC%2BD2MXht1Gqu7vL 15988575 10.1007/s00253-005-0029-3
    • Pasch JC, Nickelsen J, Schünemann D (2005) The yeast split-ubiquitin system to study chloroplast membrane protein interactions. Appl Microbiol Biotechnol 69:440-447
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 440-447
    • Pasch, J.C.1    Nickelsen, J.2    Schünemann, D.3
  • 53
    • 79961242561 scopus 로고    scopus 로고
    • Model for membrane organization and protein sorting in the cyanobacterium Synechocystis sp. PCC 6803 inferred from proteomics and multivariate sequence analyses
    • 1:CAS:528:DC%2BC3MXotVaktr8%3D 21648951 10.1021/pr200268r
    • Pisareva T, Kwon J, Oh J, Kim S, Ge C, Wieslander A, Choi JS, Norling B (2011) Model for membrane organization and protein sorting in the cyanobacterium Synechocystis sp. PCC 6803 inferred from proteomics and multivariate sequence analyses. J Proteome Res 10:3617-3631
    • (2011) J Proteome Res , vol.10 , pp. 3617-3631
    • Pisareva, T.1    Kwon, J.2    Oh, J.3    Kim, S.4    Ge, C.5    Wieslander, A.6    Choi, J.S.7    Norling, B.8
  • 54
    • 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
    • 1:CAS:528:DC%2BD28XhtFSrtr3M 16923804 10.1074/jbc.M606360200
    • Promnares K, Komenda J, Bumba L, Nebesarova J, Vacha F, 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
    • (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
  • 55
    • 33144469231 scopus 로고    scopus 로고
    • Primary electron transfer
    • T.J. Wydrzynski K. Satoh (eds) Advances in photosynthesis and respiration series 22 Springer Dordrecht
    • Renger G, Holzwart AR (2005) Primary electron transfer. In: Wydrzynski TJ, Satoh K (eds) Photosystem II: The light-driven water: plastoquinone oxidoreductase, vol 22., Advances in photosynthesis and respiration series. Springer, Dordrecht, pp 139-175
    • (2005) Photosystem II: The Light-driven Water: Plastoquinone Oxidoreductase , pp. 139-175
    • Renger, G.1    Holzwart, A.R.2
  • 56
    • 77952413469 scopus 로고    scopus 로고
    • Rapid dark repression of 5-aminolevulinic acid synthesis in green barley leaves
    • 1:CAS:528:DC%2BC3cXmtFOgsLc%3D 20375109 10.1093/pcp/pcq047
    • Richter A, Peter E, Pörs Y, Lorenzen S, Grimm B, Czarnecki O (2010) Rapid dark repression of 5-aminolevulinic acid synthesis in green barley leaves. Plant Cell Physiol 51:670-681
    • (2010) Plant Cell Physiol , vol.51 , pp. 670-681
    • Richter, A.1    Peter, E.2    Pörs, Y.3    Lorenzen, S.4    Grimm, B.5    Czarnecki, O.6
  • 57
    • 23844488456 scopus 로고    scopus 로고
    • Enzymes of the last steps of chlorophyll biosynthesis: Modification of the substrate structure helps to understand the topology of the active centers
    • 16086589 10.1021/bi0504198
    • Rüdiger W, Böhm S, Helfrich M, Schulz S, Schoch S (2005) Enzymes of the last steps of chlorophyll biosynthesis: modification of the substrate structure helps to understand the topology of the active centers. Biochemistry 44:10864-10872
    • (2005) Biochemistry , vol.44 , pp. 10864-10872
    • Rüdiger, W.1    Böhm, S.2    Helfrich, M.3    Schulz, S.4    Schoch, S.5
  • 58
    • 84869785862 scopus 로고    scopus 로고
    • Biogenic membranes of the chloroplast in Chlamydomonas reinhardtii
    • 1:CAS:528:DC%2BC38XhvVagtrbN 23129655 10.1073/pnas.1209860109
    • Schottkowski M, Peters M, Zhan Y, Rifai O, Zhang Y, Zerges W (2012) Biogenic membranes of the chloroplast in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 109:19286-19291
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19286-19291
    • Schottkowski, M.1    Peters, M.2    Zhan, Y.3    Rifai, O.4    Zhang, Y.5    Zerges, W.6
  • 59
    • 24644520415 scopus 로고    scopus 로고
    • Kinetic basis for linking the first two enzymes of chlorophyll biosynthesis
    • 1:CAS:528:DC%2BD2MXhtVWisrjL 16128821 10.1111/j.1742-4658.2005.04873.x
    • Shepherd M, McLean S, Hunter CN (2005) Kinetic basis for linking the first two enzymes of chlorophyll biosynthesis. FEBS J 272:4532-4539
    • (2005) FEBS J , vol.272 , pp. 4532-4539
    • Shepherd, M.1    McLean, S.2    Hunter, C.N.3
  • 60
    • 0001002387 scopus 로고
    • Biosynthesis of chlorophyll b
    • 1:CAS:528:DyaE3MXkslansro%3D 10.1146/annurev.pp.22.060171.001125
    • Shlyk AA (1971) Biosynthesis of chlorophyll b. Annu Rev Plant Physiol 22:169-184
    • (1971) Annu Rev Plant Physiol , vol.22 , pp. 169-184
    • Shlyk, A.A.1
  • 61
    • 84857998566 scopus 로고    scopus 로고
    • Small CAB-like proteins prevent formation of singlet oxygen in the damaged photosystem II complex of the cyanobacterium Synechocystis sp. PCC 6803
    • 1:CAS:528:DC%2BC38XmtFWlsL4%3D 22070528 10.1111/j.1365-3040.2011.02454.x
    • Sinha RK, Komenda J, Knoppová J, Sedlářová M, Pospíšil P (2012) Small CAB-like proteins prevent formation of singlet oxygen in the damaged photosystem II complex of the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Environ 35:806-818
    • (2012) Plant Cell Environ , vol.35 , pp. 806-818
    • Sinha, R.K.1    Komenda, J.2    Knoppová, J.3    Sedlářová, M.4    Pospíšil, P.5
  • 62
    • 24744469008 scopus 로고    scopus 로고
    • Photosystem II assembly in CP47 mutant of Synechocystis sp. PCC 6803 is dependent on the level of chlorophyll precursors regulated by ferrochelatase
    • 1:CAS:528:DC%2BD2MXpslejsr8%3D 16027152 10.1074/jbc.M505976200
    • Sobotka R, Komenda J, Bumba L, Tichy M (2005) Photosystem II assembly in CP47 mutant of Synechocystis sp. PCC 6803 is dependent on the level of chlorophyll precursors regulated by ferrochelatase. J Biol Chem 280:31595-31602
    • (2005) J Biol Chem , vol.280 , pp. 31595-31602
    • Sobotka, R.1    Komenda, J.2    Bumba, L.3    Tichy, M.4
  • 63
    • 54449102004 scopus 로고    scopus 로고
    • Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes
    • 1:CAS:528:DC%2BD1cXhtFSltL3I 18625715 10.1074/jbc.M803787200
    • Sobotka R, Dühring U, Komenda J, Peter E, Gardian Z, Tichý M, Grimm B, Wilde A (2008a) Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes. J Biol Chem 283:25794-25802
    • (2008) J Biol Chem , vol.283 , pp. 25794-25802
    • Sobotka, R.1    Dühring, U.2    Komenda, J.3    Peter, E.4    Gardian, Z.5    Tichý, M.6    Grimm, B.7    Wilde, A.8
  • 64
    • 40449091817 scopus 로고    scopus 로고
    • The C-terminal extension of ferrochelatase is critical for enzyme activity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803
    • 1:CAS:528:DC%2BD1cXjtFCns70%3D 2258870 18192382 10.1128/JB.01678-07
    • Sobotka R, McLean S, Zuberova M, Hunter CN, Tichy M (2008b) The C-terminal extension of ferrochelatase is critical for enzyme activity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803. J Bacteriol 190:2086-2095
    • (2008) J Bacteriol , vol.190 , pp. 2086-2095
    • Sobotka, R.1    McLean, S.2    Zuberova, M.3    Hunter, C.N.4    Tichy, M.5
  • 65
    • 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
    • 1:CAS:528:DC%2BC3MXkvVOrtr0%3D 3091120 21081693 10.1104/pp.110.167528
    • Sobotka R, Tichy M, Wilde A, Hunter CN (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
    • (2011) Plant Physiol , vol.155 , pp. 1735-1747
    • Sobotka, R.1    Tichy, M.2    Wilde, A.3    Hunter, C.N.4
  • 66
    • 77952372524 scopus 로고    scopus 로고
    • Involvement of carotenoids in the synthesis and assembly of protein subunits of photosynthetic reaction centers of Synechocystis sp. PCC 6803
    • 1:CAS:528:DC%2BC3cXmtFOgs7o%3D 20231245 10.1093/pcp/pcq031
    • Sozer O, Komenda J, Ughy B, Domonkos I, Laczkó-Dobos H, Malec P, Gombos Z, Kis M (2010) Involvement of carotenoids in the synthesis and assembly of protein subunits of photosynthetic reaction centers of Synechocystis sp. PCC 6803. Plant Cell Physiol 51:823-835
    • (2010) Plant Cell Physiol , vol.51 , pp. 823-835
    • Sozer, O.1    Komenda, J.2    Ughy, B.3    Domonkos, I.4    Laczkó-Dobos, H.5    Malec, P.6    Gombos, Z.7    Kis, M.8
  • 67
    • 11244280870 scopus 로고    scopus 로고
    • A homolog of Albino3/OxaI is essential for thylakoid biogenesis in the cyanobacterium Synechocystis sp. PCC6803
    • 1:CAS:528:DC%2BD2cXhtFeis7fL 15498761 10.1074/jbc.M411041200
    • Spence E, Bailey S, Nenninger A, Møller SG, Robinson C (2004) A homolog of Albino3/OxaI is essential for thylakoid biogenesis in the cyanobacterium Synechocystis sp. PCC6803. J Biol Chem 279:55792-55800
    • (2004) J Biol Chem , vol.279 , pp. 55792-55800
    • Spence, E.1    Bailey, S.2    Nenninger, A.3    Møller, S.G.4    Robinson, C.5
  • 68
    • 84859080796 scopus 로고    scopus 로고
    • Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis
    • 1:CAS:528:DC%2BC38Xns1els7w%3D 3315239 22319052 10.1105/tpc.111.093914
    • Stengel A, Gügel IL, Hilger D, Rengstl B, Jung H, Nickelsen J (2012) Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis. Plant Cell 24:660-675
    • (2012) Plant Cell , vol.24 , pp. 660-675
    • Stengel, A.1    Gügel, I.L.2    Hilger, D.3    Rengstl, B.4    Jung, H.5    Nickelsen, J.6
  • 69
    • 53149094046 scopus 로고    scopus 로고
    • A conserved structure and function of the YidC homologous protein Slr1471 from Synechocystis sp. PCC 6803
    • 18600052
    • Sven G, Eva R, Uwe K, Schneider D (2008) A conserved structure and function of the YidC homologous protein Slr1471 from Synechocystis sp. PCC 6803. J Microbiol Biotechnol 18:1090-1094
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1090-1094
    • Sven, G.1    Eva, R.2    Uwe, K.3    Schneider, D.4
  • 70
    • 34250807129 scopus 로고    scopus 로고
    • Tetrapyrrole biosynthesis in higher plants
    • 1:CAS:528:DC%2BD2sXnsVahsL0%3D 17227226 10.1146/annurev.arplant.57. 032905.105448
    • Tanaka R, Tanaka A (2007) Tetrapyrrole biosynthesis in higher plants. Annu Rev Plant Biol 58:321-346
    • (2007) Annu Rev Plant Biol , vol.58 , pp. 321-346
    • Tanaka, R.1    Tanaka, A.2
  • 71
    • 0035040683 scopus 로고    scopus 로고
    • Regulation of translation elongation in cyanobacteria: Membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein
    • 11309129 10.1046/j.1365-2958.2001.02402.x
    • Tyystjärvi T, Herranen M, Aro EM (2001) Regulation of translation elongation in cyanobacteria: membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein. Mol Microbiol 40:476-484
    • (2001) Mol Microbiol , vol.40 , pp. 476-484
    • Tyystjärvi, T.1    Herranen, M.2    Aro, E.M.3
  • 73
    • 34447092491 scopus 로고    scopus 로고
    • Continuous chlorophyll degradation accompanied by chlorophyllide and phytol reutilization for chlorophyll synthesis in Synechocystis sp. PCC 6803
    • 1:CAS:528:DC%2BD2sXnslWhu7c%3D 17499209 10.1016/j.bbabio.2007.03.010
    • Vavilin D, Vermaas WFJ (2007) Continuous chlorophyll degradation accompanied by chlorophyllide and phytol reutilization for chlorophyll synthesis in Synechocystis sp. PCC 6803. Biochim Biophys Acta 1767:920-929
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 920-929
    • Vavilin, D.1    Vermaas, W.F.J.2
  • 74
    • 22244479011 scopus 로고    scopus 로고
    • 15N-labeling to determine chlorophyll synthesis and degradation in Synechocystis sp. PCC 6803 strains lacking one or both photosystems
    • 1:CAS:528:DC%2BD2MXltFSktbY%3D 15949987 10.1016/j.bbabio.2004.12.011
    • 15N-labeling to determine chlorophyll synthesis and degradation in Synechocystis sp. PCC 6803 strains lacking one or both photosystems. Biochim Biophys Acta 1708:91-101
    • (2005) Biochim Biophys Acta , vol.1708 , pp. 91-101
    • Vavilin, D.1    Brune, D.C.2    Vermaas, W.F.J.3
  • 76
    • 84863407242 scopus 로고    scopus 로고
    • Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle
    • 1:CAS:528:DC%2BC38XhvFGrtbY%3D 3268725 22160593 10.1091/mbc.E11-07-0590
    • Welte T, Kudva R, Kuhn P, Sturm L, Braig D, Müller M, Warscheid B, Drepper F, Koch HG (2012) Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle. Mol Biol Cell 23:464-479
    • (2012) Mol Biol Cell , vol.23 , pp. 464-479
    • Welte, T.1    Kudva, R.2    Kuhn, P.3    Sturm, L.4    Braig, D.5    Müller, M.6    Warscheid, B.7    Drepper, F.8    Koch, H.G.9
  • 77
    • 0036050398 scopus 로고    scopus 로고
    • The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • 1:CAS:528:DC%2BD38XlslKlurk%3D 12100545 10.1046/j.1365-2958.2002.02993.x
    • Woldringh CL (2002) The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation. Mol Microbiol 45:17-29
    • (2002) Mol Microbiol , vol.45 , pp. 17-29
    • Woldringh, C.L.1
  • 78
    • 33751079088 scopus 로고    scopus 로고
    • Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana
    • 1:CAS:528:DC%2BD28Xht1ejurbO 1630749 17028153 10.1104/pp.106.086090
    • Yamazaki S, Nomata J, Fujita Y (2006) Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana. Plant Physiol 142:911-922
    • (2006) Plant Physiol , vol.142 , pp. 911-922
    • Yamazaki, S.1    Nomata, J.2    Fujita, Y.3
  • 79
    • 84855258509 scopus 로고    scopus 로고
    • Photosystem II component lifetimes in the cyanobacterium Synechocystis sp strain PCC 6803: Small Cab-like proteins stabilize biosynthesis intermediates and affect early steps in chlorophyll synthesis
    • 1:CAS:528:DC%2BC38XotVGl 22090028 10.1074/jbc.M111.320994
    • Yao DC, Brune DC, Vavilin D, Vermaas WFJ (2012) Photosystem II component lifetimes in the cyanobacterium Synechocystis sp. strain PCC 6803: small Cab-like proteins stabilize biosynthesis intermediates and affect early steps in chlorophyll synthesis. J Biol Chem 287:682-692
    • (2012) J Biol Chem , vol.287 , pp. 682-692
    • Yao, D.C.1    Brune, D.C.2    Vavilin, D.3    Vermaas, W.F.J.4
  • 80
    • 0035851097 scopus 로고    scopus 로고
    • A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis
    • 1:CAS:528:DC%2BD3MXotFOrtrg%3D 11473124
    • Zhang L, Paakkarinen V, Suorsa M, Aro EM (2001) A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis. J Biol Chem 276:37809-37814
    • (2001) J Biol Chem , vol.276 , pp. 37809-37814
    • Zhang, L.1    Paakkarinen, V.2    Suorsa, M.3    Aro, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.