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Volumn 19, Issue 4, 2007, Pages 1329-1346

The nuclear-encoded factor HCF173 Is involved in the initiation of translation of the psbA mRNA in Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; MUTAGENESIS; PLANTS (BOTANY); PROTEINS;

EID: 34250657285     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.106.042895     Document Type: Article
Times cited : (86)

References (81)
  • 1
    • 0032524468 scopus 로고    scopus 로고
    • Characterization of protein-binding to the spinach chloroplast psbA mRNA 5′ untranslated region
    • Alexander, C., Faber, N., and Klaff, P. (1998). Characterization of protein-binding to the spinach chloroplast psbA mRNA 5′ untranslated region. Nucleic Acids Res. 26: 2265-2272.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2265-2272
    • Alexander, C.1    Faber, N.2    Klaff, P.3
  • 2
  • 3
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro, E.M., Virgin, I., and Andersson, B. (1993). Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta 1143: 113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 4
    • 2342456308 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Terminating erroneous gene expression
    • Baker, K.E., and Parker, R. (2004). Nonsense-mediated mRNA decay: Terminating erroneous gene expression. Curr. Opin. Cell Biol. 16: 293-299.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 293-299
    • Baker, K.E.1    Parker, R.2
  • 5
    • 0032551718 scopus 로고    scopus 로고
    • Spinach CSP41, an mRNA-binding protein and ribonuclease, is homologous to nucleotide-sugar epimerases and hydroxysteroid dehydrogenases
    • Baker, M.E., Grundy, W.N., and Elkan, C.P. (1998). Spinach CSP41, an mRNA-binding protein and ribonuclease, is homologous to nucleotide-sugar epimerases and hydroxysteroid dehydrogenases. Biochem. Biophys. Res. Commun. 248: 250-254.
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 250-254
    • Baker, M.E.1    Grundy, W.N.2    Elkan, C.P.3
  • 6
    • 0001829914 scopus 로고
    • Nuclear mutants of maize with defects in chloroplast polysome assembly have altered chloroplast RNA metabolism
    • Barkan, A. (1993). Nuclear mutants of maize with defects in chloroplast polysome assembly have altered chloroplast RNA metabolism. Plant Cell 5: 389-402.
    • (1993) Plant Cell , vol.5 , pp. 389-402
    • Barkan, A.1
  • 7
    • 0033860532 scopus 로고    scopus 로고
    • Participation of nuclear genes in chloroplast gene expression
    • Barkan, A., and Goldschmidt-Clermont, M. (2000). Participation of nuclear genes in chloroplast gene expression. Biochimie 82: 559-572.
    • (2000) Biochimie , vol.82 , pp. 559-572
    • Barkan, A.1    Goldschmidt-Clermont, M.2
  • 8
    • 3142655271 scopus 로고    scopus 로고
    • Identification and characterization of a novel RNA binding protein that associates with the 59-untranslated region of the chloroplast psbA mRNA
    • Barnes, D., Cohen, A., Bruick, R.K., Kantardjieff, K., Fowler, S., Efuet, E., and Mayfield, S.P. (2004). Identification and characterization of a novel RNA binding protein that associates with the 59-untranslated region of the chloroplast psbA mRNA. Biochemistry 43: 8541-8550.
    • (2004) Biochemistry , vol.43 , pp. 8541-8550
    • Barnes, D.1    Cohen, A.2    Bruick, R.K.3    Kantardjieff, K.4    Fowler, S.5    Efuet, E.6    Mayfield, S.P.7
  • 9
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman, A., et al. (2004). The Pfam protein families database. Nucleic Acids Res. 32: D138-D141.
    • (2004) Nucleic Acids Res , vol.32
    • Bateman, A.1
  • 10
    • 0028055069 scopus 로고
    • Assignment of 30 microsatellite loci to the linkage map of Arabidopsis
    • Bell, C.J., and Ecker, J.R. (1994). Assignment of 30 microsatellite loci to the linkage map of Arabidopsis. Genomics 19: 137-144.
    • (1994) Genomics , vol.19 , pp. 137-144
    • Bell, C.J.1    Ecker, J.R.2
  • 11
    • 11344256503 scopus 로고    scopus 로고
    • Cooperation of endo- and exoribonucleases in chloroplast mRNA turnover
    • Bollenbach, T.J., Schuster, G., and Stern, D.B. (2004). Cooperation of endo- and exoribonucleases in chloroplast mRNA turnover. Prog. Nucleic Acid Res. Mol. Biol. 78: 305-337.
    • (2004) Prog. Nucleic Acid Res. Mol. Biol , vol.78 , pp. 305-337
    • Bollenbach, T.J.1    Schuster, G.2    Stern, D.B.3
  • 12
    • 0043163808 scopus 로고    scopus 로고
    • Divalent metal-dependent catalysis and cleavage specificity of CSP41, a chloroplast endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily
    • Bollenbach, T.J., and Stern, D.B. (2003). Divalent metal-dependent catalysis and cleavage specificity of CSP41, a chloroplast endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily. Nucleic Acids Res. 31: 4317-4325.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4317-4325
    • Bollenbach, T.J.1    Stern, D.B.2
  • 13
    • 0037010174 scopus 로고    scopus 로고
    • Translational regulations as specific traits of chloroplast gene expression
    • Choquet, Y., and Wollman, F.A. (2002). Translational regulations as specific traits of chloroplast gene expression. FEBS Lett. 529: 39-42.
    • (2002) FEBS Lett , vol.529 , pp. 39-42
    • Choquet, Y.1    Wollman, F.A.2
  • 14
    • 0019412749 scopus 로고
    • Separation and characterization of inner and outer envelope membranes of pea chloroplasts
    • Cline, K., Andrews, J., Mersey, B., Newcomb, E.H., and Keegstra, K. (1981). Separation and characterization of inner and outer envelope membranes of pea chloroplasts. Proc. Natl. Acad. Sci. USA 78: 3595-3599.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3595-3599
    • Cline, K.1    Andrews, J.2    Mersey, B.3    Newcomb, E.H.4    Keegstra, K.5
  • 15
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998). Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 16
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff, J.A., and Barton, G.J. (2000). Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40: 502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 17
    • 0025932162 scopus 로고
    • Light regulated translational activators: Identification of chloroplast gene specific mRNA binding proteins
    • Danon, A., and Mayfield, S.P. (1991). Light regulated translational activators: Identification of chloroplast gene specific mRNA binding proteins. EMBO J. 10: 3993-4001.
    • (1991) EMBO J , vol.10 , pp. 3993-4001
    • Danon, A.1    Mayfield, S.P.2
  • 18
    • 0023647945 scopus 로고
    • Control of plastid gene expression during development: The limited role of transcriptional regulation
    • Deng, X.W., and Gruissem, W. (1987). Control of plastid gene expression during development: The limited role of transcriptional regulation. Cell 49: 379-387.
    • (1987) Cell , vol.49 , pp. 379-387
    • Deng, X.W.1    Gruissem, W.2
  • 19
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G. (1999). ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8: 978-984.
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Heijne, G.3
  • 21
    • 0033522445 scopus 로고    scopus 로고
    • Molecular cloning of the maize gene crp1 reveals similarity between regulators of mitochondrial and chloroplast gene expression
    • Fisk, D.G., Walker, M.B., and Barkan, A. (1999). Molecular cloning of the maize gene crp1 reveals similarity between regulators of mitochondrial and chloroplast gene expression. EMBO J. 18: 2621-2630.
    • (1999) EMBO J , vol.18 , pp. 2621-2630
    • Fisk, D.G.1    Walker, M.B.2    Barkan, A.3
  • 22
    • 0024961946 scopus 로고
    • Translation and stability of proteins encoded by the plastid psbA and psbB genes are regulated by a nuclear gene during light-induced chloroplast development in barley
    • Gamble, P.E., and Mullet, J.E. (1989). Translation and stability of proteins encoded by the plastid psbA and psbB genes are regulated by a nuclear gene during light-induced chloroplast development in barley. J. Biol. Chem. 264: 7236-7243.
    • (1989) J. Biol. Chem , vol.264 , pp. 7236-7243
    • Gamble, P.E.1    Mullet, J.E.2
  • 23
    • 0030781424 scopus 로고    scopus 로고
    • Coordination of nuclear and chloroplast gene expression in plant cells
    • Goldschmidt-Clermont, M. (1998). Coordination of nuclear and chloroplast gene expression in plant cells. Int. Rev. Cytol. 177: 115-180.
    • (1998) Int. Rev. Cytol , vol.177 , pp. 115-180
    • Goldschmidt-Clermont, M.1
  • 24
    • 0028209999 scopus 로고
    • Enzymes as RNA-binding proteins: A role for (di)nucleotide-binding domains?
    • Hentze, M.W. (1994). Enzymes as RNA-binding proteins: A role for (di)nucleotide-binding domains? Trends Biochem. Sci. 19: 101-103.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 101-103
    • Hentze, M.W.1
  • 25
    • 0029971659 scopus 로고    scopus 로고
    • Cis-acting elements and transacting factors for accurate translation of chloroplast psbA mRNAs: Development of an in vitro translation system from tobacco chloroplasts
    • Hirose, T., and Sugiura, M. (1996). Cis-acting elements and transacting factors for accurate translation of chloroplast psbA mRNAs: Development of an in vitro translation system from tobacco chloroplasts. EMBO J. 15: 1687-1695.
    • (1996) EMBO J , vol.15 , pp. 1687-1695
    • Hirose, T.1    Sugiura, M.2
  • 26
    • 84856980739 scopus 로고    scopus 로고
    • Protein subcellular localization prediction with WoLF PSORT
    • T. Jiang, U.-C. Yang, Y.-P. Phoebe Chen, and L. Wong, eds London: Imperial College Press, pp
    • Horton, P., Park, K.-J., Obayashi, T., and Nakai, K. (2006). Protein subcellular localization prediction with WoLF PSORT. In Proceedings of the 4th Asia-Pacific Bioinformatics Conference (APBC2006), T. Jiang, U.-C. Yang, Y.-P. Phoebe Chen, and L. Wong, eds (London: Imperial College Press), pp. 39-48.
    • (2006) Proceedings of the 4th Asia-Pacific Bioinformatics Conference (APBC2006) , pp. 39-48
    • Horton, P.1    Park, K.-J.2    Obayashi, T.3    Nakai, K.4
  • 30
    • 0036809427 scopus 로고    scopus 로고
    • The active site of the thioredoxin-like domain of chloroplast protein disulfide isomerase, RB60, catalyzes the redox-regulated binding of chloroplast poly(A)-binding protein, RB47, to the 5′ untranslated region of psbA mRNA
    • Kim, J., and Mayfield, S.P. (2002). The active site of the thioredoxin-like domain of chloroplast protein disulfide isomerase, RB60, catalyzes the redox-regulated binding of chloroplast poly(A)-binding protein, RB47, to the 5′ untranslated region of psbA mRNA. Plant Cell Physiol. 43: 1238-1243.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1238-1243
    • Kim, J.1    Mayfield, S.P.2
  • 31
    • 0027617142 scopus 로고
    • Direct evidence for selective modulation of psbA, rpoA, rbcL and 16S RNA stability during barley chloroplast development
    • Kim, M., Christopher, D.A., and Mullet, J.E. (1993). Direct evidence for selective modulation of psbA, rpoA, rbcL and 16S RNA stability during barley chloroplast development. Plant Mol. Biol. 22: 447-463.
    • (1993) Plant Mol. Biol , vol.22 , pp. 447-463
    • Kim, M.1    Christopher, D.A.2    Mullet, J.E.3
  • 32
    • 0002733372 scopus 로고
    • Changes in chloroplast mRNA stability during leaf development
    • Klaff, P., and Gruissem, W. (1991). Changes in chloroplast mRNA stability during leaf development. Plant Cell 3: 517-529.
    • (1991) Plant Cell , vol.3 , pp. 517-529
    • Klaff, P.1    Gruissem, W.2
  • 33
    • 0031467566 scopus 로고    scopus 로고
    • Complex formation of the spinach chloroplast psbA mRNA 5′ untranslated region with proteins is dependent on the RNA structure
    • Klaff, P., Mundt, S.M., and Steger, G. (1997). Complex formation of the spinach chloroplast psbA mRNA 5′ untranslated region with proteins is dependent on the RNA structure. RNA 3: 1468-1479.
    • (1997) RNA , vol.3 , pp. 1468-1479
    • Klaff, P.1    Mundt, S.M.2    Steger, G.3
  • 34
    • 0023881275 scopus 로고
    • Light-regulated translation of chloroplast proteins. I. Transcripts of psaA-psaB, psbA, and rbcL are associated with polysomes in dark-grown and illuminated barley seedlings
    • Klein, R.R., Mason, H.S., and Mullet, J.E. (1988). Light-regulated translation of chloroplast proteins. I. Transcripts of psaA-psaB, psbA, and rbcL are associated with polysomes in dark-grown and illuminated barley seedlings. J. Cell Biol. 106: 289-301.
    • (1988) J. Cell Biol , vol.106 , pp. 289-301
    • Klein, R.R.1    Mason, H.S.2    Mullet, J.E.3
  • 35
    • 0025182348 scopus 로고
    • Light-induced transcription of chloroplast genes. psbA transcription is differentially enhanced in illuminated barley
    • Klein, R.R., and Mullet, J.E. (1990). Light-induced transcription of chloroplast genes. psbA transcription is differentially enhanced in illuminated barley. J. Biol. Chem. 265: 1895-1902.
    • (1990) J. Biol. Chem , vol.265 , pp. 1895-1902
    • Klein, R.R.1    Mullet, J.E.2
  • 36
    • 0027650566 scopus 로고
    • A procedure for mapping Arabidopsis mutations using co-dominant ecotype-specific PCR-based markers
    • Konieczny, A., and Ausubel, F.M. (1993). A procedure for mapping Arabidopsis mutations using co-dominant ecotype-specific PCR-based markers. Plant J. 4: 403-410.
    • (1993) Plant J , vol.4 , pp. 403-410
    • Konieczny, A.1    Ausubel, F.M.2
  • 37
    • 0345306693 scopus 로고    scopus 로고
    • From genes to photosynthesis in Arabidopsis thaliana
    • Leister, D., and Schneider, A. (2003). From genes to photosynthesis in Arabidopsis thaliana. Int. Rev. Cytol. 228: 31-83.
    • (2003) Int. Rev. Cytol , vol.228 , pp. 31-83
    • Leister, D.1    Schneider, A.2
  • 38
    • 0035209897 scopus 로고    scopus 로고
    • HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis
    • Lennartz, K., Plücken, H., Seidler, A., Westhoff, P., Bechtold, N., and Meierhoff, K. (2001). HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis. Plant Cell 13: 2539-2551.
    • (2001) Plant Cell , vol.13 , pp. 2539-2551
    • Lennartz, K.1    Plücken, H.2    Seidler, A.3    Westhoff, P.4    Bechtold, N.5    Meierhoff, K.6
  • 40
    • 0029991899 scopus 로고    scopus 로고
    • Fully edited and partially edited nad9 transcripts differ in size and both are associated with polysomes in potato mitochondria
    • Lu, B., and Hanson, M.R. (1996). Fully edited and partially edited nad9 transcripts differ in size and both are associated with polysomes in potato mitochondria. Nucleic Acids Res. 24: 1369-1374.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1369-1374
    • Lu, B.1    Hanson, M.R.2
  • 41
    • 13444262384 scopus 로고    scopus 로고
    • CDD: A Conserved Domain Database for protein classification
    • Marchler-Bauer, A., et al. (2005). CDD: A Conserved Domain Database for protein classification. Nucleic Acids Res. 33: D192-D196.
    • (2005) Nucleic Acids Res , vol.33
    • Marchler-Bauer, A.1
  • 42
    • 0030199295 scopus 로고    scopus 로고
    • A nuclear mutant of Arabidopsis with impaired stability on distinct transcripts of the plastid psbB, psbD/C, ndhH, and ndhC operons
    • Meurer, J., Berger, A., and Westhoff, P. (1996a). A nuclear mutant of Arabidopsis with impaired stability on distinct transcripts of the plastid psbB, psbD/C, ndhH, and ndhC operons. Plant Cell 8: 1193-1207.
    • (1996) Plant Cell , vol.8 , pp. 1193-1207
    • Meurer, J.1    Berger, A.2    Westhoff, P.3
  • 43
    • 0030066836 scopus 로고    scopus 로고
    • Isolation of high-chlorophyll-fluorescence mutants of Arabidopsis thaliana and their characterisation by spectroscopy, immunoblotting and northern hybridisation
    • Meurer, J., Meierhoff, K., and Westhoff, P. (1996b). Isolation of high-chlorophyll-fluorescence mutants of Arabidopsis thaliana and their characterisation by spectroscopy, immunoblotting and northern hybridisation. Planta 198: 385-396.
    • (1996) Planta , vol.198 , pp. 385-396
    • Meurer, J.1    Meierhoff, K.2    Westhoff, P.3
  • 44
    • 0344404400 scopus 로고    scopus 로고
    • A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana
    • Meurer, J., Plücken, H., Kowallik, K.V., and Westhoff, P. (1998). A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana. EMBO J. 17: 5286-5297.
    • (1998) EMBO J , vol.17 , pp. 5286-5297
    • Meurer, J.1    Plücken, H.2    Kowallik, K.V.3    Westhoff, P.4
  • 45
    • 0002629279 scopus 로고
    • The use of mutations to probe photosynthesis in higher plants
    • M. Edelman, R. Hallick, and N.-H. Chua, eds Amsterdam: Elsevier Biomedical Press, pp
    • Miles, D. (1982). The use of mutations to probe photosynthesis in higher plants. In Methods in Chloroplast Molecular Biology, M. Edelman, R. Hallick, and N.-H. Chua, eds (Amsterdam: Elsevier Biomedical Press), pp. 75-107.
    • (1982) Methods in Chloroplast Molecular Biology , pp. 75-107
    • Miles, D.1
  • 46
    • 33645728659 scopus 로고    scopus 로고
    • Chloroplast biogenesis of photosystem II cores involves a series of assembly-controlled steps that regulate translation
    • Minai, L., Wostrikoff, K., Wollman, F.A., and Choquet, Y. (2006). Chloroplast biogenesis of photosystem II cores involves a series of assembly-controlled steps that regulate translation. Plant Cell 18: 159-175.
    • (2006) Plant Cell , vol.18 , pp. 159-175
    • Minai, L.1    Wostrikoff, K.2    Wollman, F.A.3    Choquet, Y.4
  • 47
    • 0033861250 scopus 로고    scopus 로고
    • Processing and degradation of chloroplast mRNA
    • Monde, R.A., Schuster, G., and Stern, D.B. (2000). Processing and degradation of chloroplast mRNA. Biochimie 82: 573-582.
    • (2000) Biochimie , vol.82 , pp. 573-582
    • Monde, R.A.1    Schuster, G.2    Stern, D.B.3
  • 48
    • 0034726714 scopus 로고    scopus 로고
    • Identification of the NAD(p)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain
    • Nagy, E., Henics, T., Eckert, M., Miseta, A., Lightowlers, R.N., and Kellermayer, M. (2000). Identification of the NAD(p)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain. Biochem. Biophys. Res. Commun. 275: 253-260.
    • (2000) Biochem. Biophys. Res. Commun , vol.275 , pp. 253-260
    • Nagy, E.1    Henics, T.2    Eckert, M.3    Miseta, A.4    Lightowlers, R.N.5    Kellermayer, M.6
  • 49
    • 0142088891 scopus 로고    scopus 로고
    • RNA-binding properties of HCF152, an Arabidopsis PPR protein involved in the processing of chloroplast RNA
    • Nakamura, T., Meierhoff, K., Westhoff, P., and Schuster, G. (2003). RNA-binding properties of HCF152, an Arabidopsis PPR protein involved in the processing of chloroplast RNA. Eur. J. Biochem. 270: 4070-4081.
    • (2003) Eur. J. Biochem , vol.270 , pp. 4070-4081
    • Nakamura, T.1    Meierhoff, K.2    Westhoff, P.3    Schuster, G.4
  • 50
    • 0033133576 scopus 로고    scopus 로고
    • Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas
    • Nickelsen, J., Fleischmann, M., Boudreau, E., Rahire, M., and Rochaix, J.D. (1999). Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas. Plant Cell 11: 957-970.
    • (1999) Plant Cell , vol.11 , pp. 957-970
    • Nickelsen, J.1    Fleischmann, M.2    Boudreau, E.3    Rahire, M.4    Rochaix, J.D.5
  • 52
    • 0036037428 scopus 로고    scopus 로고
    • A chloroplast RNA binding protein from stromal thylakoid membranes specifically binds to the 5′ untranslated region of the psbA mRNA
    • Ossenbühl, F., Hartmann, K., and Nickelsen, J. (2002). A chloroplast RNA binding protein from stromal thylakoid membranes specifically binds to the 5′ untranslated region of the psbA mRNA. Eur. J. Biochem. 269: 3912-3919.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3912-3919
    • Ossenbühl, F.1    Hartmann, K.2    Nickelsen, J.3
  • 53
    • 0033776506 scopus 로고    scopus 로고
    • cis- and trans-acting determinants for translation of psbD mRNA in Chlamydomonas reinhardtii
    • Ossenbühl, F., and Nickelsen, J. (2000). cis- and trans-acting determinants for translation of psbD mRNA in Chlamydomonas reinhardtii. Mol. Cell. Biol. 20: 8134-8142.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 8134-8142
    • Ossenbühl, F.1    Nickelsen, J.2
  • 54
    • 0042525906 scopus 로고    scopus 로고
    • Group II intron splicing factors derived by diversification of an ancient RNA-binding domain
    • Ostheimer, G.J., Williams-Carrier, R., Belcher, S., Osborne, E., Gierke, J., and Barkan, A. (2003). Group II intron splicing factors derived by diversification of an ancient RNA-binding domain. EMBO J. 22: 3919-3929.
    • (2003) EMBO J , vol.22 , pp. 3919-3929
    • Ostheimer, G.J.1    Williams-Carrier, R.2    Belcher, S.3    Osborne, E.4    Gierke, J.5    Barkan, A.6
  • 55
    • 0037021444 scopus 로고    scopus 로고
    • The HCF136 protein is essential for assembly of the photosystem II reaction center in Arabidopsis thaliana
    • Plücken, H., Müller, B., Grohmann, D., Westhoff, P., and Eichacker, L.A. (2002). The HCF136 protein is essential for assembly of the photosystem II reaction center in Arabidopsis thaliana. FEBS Lett. 532: 85-90.
    • (2002) FEBS Lett , vol.532 , pp. 85-90
    • Plücken, H.1    Müller, B.2    Grohmann, D.3    Westhoff, P.4    Eichacker, L.A.5
  • 56
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado-Nilsson, E., Wilm, M., and Seraphin, B. (2001). The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods 24: 218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 57
    • 19544376279 scopus 로고    scopus 로고
    • Synthesis and assembly of thylakoid protein complexes. Multiple assembly steps of photosystem II
    • Rokka, A., Suorsa, M., Saleem, A., Battchikova, N., and Aro, E.M. (2005). Synthesis and assembly of thylakoid protein complexes. Multiple assembly steps of photosystem II. Biochem J. 388: 159-168.
    • (2005) Biochem J , vol.388 , pp. 159-168
    • Rokka, A.1    Suorsa, M.2    Saleem, A.3    Battchikova, N.4    Aro, E.M.5
  • 58
    • 1642465435 scopus 로고    scopus 로고
    • An Arabidopsis thaliana T-DNA mutagenized population (GABI-Kat) for flanking sequence tag-based reverse genetics
    • Rosso, M.G., Li, Y., Strizhov, N., Reiss, B., Dekker, K., and Weisshaar, B. (2003). An Arabidopsis thaliana T-DNA mutagenized population (GABI-Kat) for flanking sequence tag-based reverse genetics. Plant Mol. Biol. 53: 247-259.
    • (2003) Plant Mol. Biol , vol.53 , pp. 247-259
    • Rosso, M.G.1    Li, Y.2    Strizhov, N.3    Reiss, B.4    Dekker, K.5    Weisshaar, B.6
  • 59
    • 20444455913 scopus 로고    scopus 로고
    • The nuclear gene HCF107 encodes a membrane-associated R-TPR (RNA tetratricopeptide repeat)-containing protein involved in expression of the plastidial psbH gene in Arabidopsis
    • Sane, A.P., Stein, B., and Westhoff, P. (2005). The nuclear gene HCF107 encodes a membrane-associated R-TPR (RNA tetratricopeptide repeat)-containing protein involved in expression of the plastidial psbH gene in Arabidopsis. Plant J. 42: 720-730.
    • (2005) Plant J , vol.42 , pp. 720-730
    • Sane, A.P.1    Stein, B.2    Westhoff, P.3
  • 60
    • 0030871303 scopus 로고    scopus 로고
    • Universal template plasmid for introduction of the triple-HA epitope sequence into cloned genes
    • Sato, M.H., and Wada, Y. (1997). Universal template plasmid for introduction of the triple-HA epitope sequence into cloned genes. Biotechniques 23: 254-256.
    • (1997) Biotechniques , vol.23 , pp. 254-256
    • Sato, M.H.1    Wada, Y.2
  • 61
    • 0036013395 scopus 로고    scopus 로고
    • Regulation of gene expression by low levels of ultraviolet-B radiation in Pisum sativum: Isolation of novel genes by suppression subtractive hybridisation
    • Sävenstrand, H., Brosché , M., and Strid, A. (2002). Regulation of gene expression by low levels of ultraviolet-B radiation in Pisum sativum: Isolation of novel genes by suppression subtractive hybridisation. Plant Cell Physiol. 43: 402-410.
    • (2002) Plant Cell Physiol , vol.43 , pp. 402-410
    • Sävenstrand, H.1    Brosché, M.2    Strid, A.3
  • 62
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation ofmembrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W.A., and von Jagow, G. (1994). Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation ofmembrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217: 220-230.
    • (1994) Anal. Biochem , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 63
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 64
    • 31544432771 scopus 로고    scopus 로고
    • RNA immunoprecipitation and microarray analysis show a chloroplast pentatricopeptide repeat protein to be associated with the 5′ region of mRNAs whose translation it activates
    • Schmitz-Linneweber, C., Williams-Carrier, R., and Barkan, A. (2005). RNA immunoprecipitation and microarray analysis show a chloroplast pentatricopeptide repeat protein to be associated with the 5′ region of mRNAs whose translation it activates. Plant Cell 17: 2791-2804.
    • (2005) Plant Cell , vol.17 , pp. 2791-2804
    • Schmitz-Linneweber, C.1    Williams-Carrier, R.2    Barkan, A.3
  • 65
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P., and Ponting, C.P. (1998). SMART, a simple modular architecture research tool: Identification of signaling domains. Proc. Natl. Acad. Sci. USA 95: 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 66
    • 0034755289 scopus 로고    scopus 로고
    • RNA binding-proteins interact specifically with the Arabidopsis chloroplast psbA mRNA 5′ untranslated region in a redox-dependent manner
    • Shen, Y., Danon, A., and Christopher, D.A. (2001). RNA binding-proteins interact specifically with the Arabidopsis chloroplast psbA mRNA 5′ untranslated region in a redox-dependent manner. Plant Cell Physiol. 42: 1071-1078.
    • (2001) Plant Cell Physiol , vol.42 , pp. 1071-1078
    • Shen, Y.1    Danon, A.2    Christopher, D.A.3
  • 67
    • 0014409322 scopus 로고
    • Drosophila alcohol dehydrogenase. Purification and partial characterization
    • Sofer, W., and Ursprung, H. (1968). Drosophila alcohol dehydrogenase. Purification and partial characterization. J. Biol. Chem. 243: 3110-3115.
    • (1968) J. Biol. Chem , vol.243 , pp. 3110-3115
    • Sofer, W.1    Ursprung, H.2
  • 68
    • 18844399317 scopus 로고    scopus 로고
    • A nuclear gene of Chlamydomonas reinhardtii, Tba1, encodes a putative oxidoreductase required for translation of the chloroplast psbA mRNA
    • Somanchi, A., Barnes, D., and Mayfield, S.P. (2005). A nuclear gene of Chlamydomonas reinhardtii, Tba1, encodes a putative oxidoreductase required for translation of the chloroplast psbA mRNA. Plant J. 42: 341-352.
    • (2005) Plant J , vol.42 , pp. 341-352
    • Somanchi, A.1    Barnes, D.2    Mayfield, S.P.3
  • 69
    • 0028518530 scopus 로고
    • Translation of psbA mRNA is regulated by light via the 5′-untranslated region in tobacco plastids
    • Staub, J.M., and Maliga, P. (1994). Translation of psbA mRNA is regulated by light via the 5′-untranslated region in tobacco plastids. Plant J. 6: 547-553.
    • (1994) Plant J , vol.6 , pp. 547-553
    • Staub, J.M.1    Maliga, P.2
  • 70
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 71
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh, T., Levitan, A., Sofer, A., and Danon, A. (2000). Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol. Cell. Biol. 20: 1116-1123.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 72
    • 0034687823 scopus 로고    scopus 로고
    • Characterization of Mbb1, a nucleus-encoded tetratricopeptide-like repeat protein required for expression of the chloroplast psbB/psbT/psbH gene cluster in Chlamydomonas reinhardtii
    • Vaistij, F.E., Boudreau, E., Lemaire, S.D., Goldschmidt-Clermont, M., and Rochaix, J.D. (2000). Characterization of Mbb1, a nucleus-encoded tetratricopeptide-like repeat protein required for expression of the chloroplast psbB/psbT/psbH gene cluster in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 97: 14813-14818.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14813-14818
    • Vaistij, F.E.1    Boudreau, E.2    Lemaire, S.D.3    Goldschmidt-Clermont, M.4    Rochaix, J.D.5
  • 73
    • 0023953590 scopus 로고
    • Complex RNA maturation in chloroplasts. The psbB operon from spinach
    • Westhoff, P., and Herrmann, R.G. (1988). Complex RNA maturation in chloroplasts. The psbB operon from spinach. Eur. J. Biochem. 171: 551-564.
    • (1988) Eur. J. Biochem , vol.171 , pp. 551-564
    • Westhoff, P.1    Herrmann, R.G.2
  • 74
    • 0000691858 scopus 로고
    • Differential accumulation of plastid transcripts encoding photosystem II components in the mesophyll and bundle-sheath cells of monocotyledonous NADP-malic enzyme-type C4 plants
    • Westhoff, P., Offermann-Steinhard, K., Höfer, M., Eskins, K., Oswald, A., and Streubel, M. (1991). Differential accumulation of plastid transcripts encoding photosystem II components in the mesophyll and bundle-sheath cells of monocotyledonous NADP-malic enzyme-type C4 plants. Planta 184: 377-388.
    • (1991) Planta , vol.184 , pp. 377-388
    • Westhoff, P.1    Offermann-Steinhard, K.2    Höfer, M.3    Eskins, K.4    Oswald, A.5    Streubel, M.6
  • 75
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman, F.A., Minai, L., and Nechushtai, R. (1999). The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta 1411: 21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 76
    • 0031007946 scopus 로고    scopus 로고
    • The spinach chloroplast endoribonuclease CSP41 cleaves the 39-untranslated region of petD mRNA primarily within its terminal stem-loop structure
    • Yang, J., and Stern, D.B. (1997). The spinach chloroplast endoribonuclease CSP41 cleaves the 39-untranslated region of petD mRNA primarily within its terminal stem-loop structure. J. Biol. Chem. 272: 12874-12880.
    • (1997) J. Biol. Chem , vol.272 , pp. 12874-12880
    • Yang, J.1    Stern, D.B.2
  • 77
    • 0032478202 scopus 로고    scopus 로고
    • A poly(A) binding protein functions in the chloroplast as a messagespecific translation factor
    • Yohn, C.B., Cohen, A., Danon, A., and Mayfield, S.P. (1998a). A poly(A) binding protein functions in the chloroplast as a messagespecific translation factor. Proc. Natl. Acad. Sci. USA 95: 2238-2243.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2238-2243
    • Yohn, C.B.1    Cohen, A.2    Danon, A.3    Mayfield, S.P.4
  • 78
    • 0032572530 scopus 로고    scopus 로고
    • Translation of the chloroplast psbA mRNA requires the nuclear-encoded poly(A)-binding protein, RB47
    • Yohn, C.B., Cohen, A., Rosch, C., Kuchka, M.R., and Mayfield, S.P. (1998b). Translation of the chloroplast psbA mRNA requires the nuclear-encoded poly(A)-binding protein, RB47. J. Cell Biol. 142: 435-442.
    • (1998) J. Cell Biol , vol.142 , pp. 435-442
    • Yohn, C.B.1    Cohen, A.2    Rosch, C.3    Kuchka, M.R.4    Mayfield, S.P.5
  • 79
    • 0033851987 scopus 로고    scopus 로고
    • Translation in chloroplasts
    • Zerges, W. (2000). Translation in chloroplasts. Biochimie 82: 583-601.
    • (2000) Biochimie , vol.82 , pp. 583-601
    • Zerges, W.1
  • 80
    • 0031953257 scopus 로고    scopus 로고
    • Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii
    • Zerges, W., and Rochaix, J.D. (1998). Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii. J. Cell Biol. 140: 101-110.
    • (1998) J. Cell Biol , vol.140 , pp. 101-110
    • Zerges, W.1    Rochaix, J.D.2
  • 81
    • 0033791940 scopus 로고    scopus 로고
    • Biogenesis of the chloroplast-encoded D1 protein: Regulation of translation elongation, insertion, and assembly into photosystem II
    • Zhang, L., Paakkarinen, V., van Wijk, K.J., and Aro, E.M. (2000). Biogenesis of the chloroplast-encoded D1 protein: Regulation of translation elongation, insertion, and assembly into photosystem II. Plant Cell 12: 1769-1782.
    • (2000) Plant Cell , vol.12 , pp. 1769-1782
    • Zhang, L.1    Paakkarinen, V.2    van Wijk, K.J.3    Aro, E.M.4


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