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Volumn 1847, Issue 9, 2015, Pages 779-785

RNA editing in plants: Machinery and flexibility of site recognition

Author keywords

Abbreviations MORF multiple organellar RNA editing factor; NDH NADH dehydrogenase like (complex); PPR pentatrico peptide repeat; RIP RNA editing factor interacting protein; RRM RNA recognition motif

Indexed keywords

MULTIPLE ORGANELLAR RNA EDITING FACTOR 1; PENTATRICOPEPTIDE REPEAT; PLANT RNA; RNA EDITING FACTOR INTERACTING PROTEIN 1; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 84935006246     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.12.010     Document Type: Review
Times cited : (90)

References (67)
  • 1
    • 0037371743 scopus 로고    scopus 로고
    • Uridine insertion/deletion RNA editing in trypanosome mitochondria: a complex business
    • L. Simpson, S. Sbicego, and R. Aphasizhev Uridine insertion/deletion RNA editing in trypanosome mitochondria: a complex business RNA 9 2003 265 276
    • (2003) RNA , vol.9 , pp. 265-276
    • Simpson, L.1    Sbicego, S.2    Aphasizhev, R.3
  • 4
    • 84879678855 scopus 로고    scopus 로고
    • Comprehensive high-resolution analysis of the role of an Arabidopsis gene family in RNA editing
    • S. Bentolila, J. Oh, M.R. Hanson, and R. Bukowski Comprehensive high-resolution analysis of the role of an Arabidopsis gene family in RNA editing PLoS Genet. 9 2013 e1003584
    • (2013) PLoS Genet. , vol.9
    • Bentolila, S.1    Oh, J.2    Hanson, M.R.3    Bukowski, R.4
  • 5
    • 34249938871 scopus 로고    scopus 로고
    • Conserved domain structure of pentatricopeptide repeat proteins involved in chloroplast RNA editing
    • K. Okuda, F. Myouga, R. Motohashi, K. Shinozaki, and T. Shikanai Conserved domain structure of pentatricopeptide repeat proteins involved in chloroplast RNA editing Proc. Natl. Acad. Sci. U. S. A. 104 2007 8178 8183
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 8178-8183
    • Okuda, K.1    Myouga, F.2    Motohashi, R.3    Shinozaki, K.4    Shikanai, T.5
  • 8
    • 12744253474 scopus 로고    scopus 로고
    • A pentatricopetide repeat protein is essential for RNA editing in chloroplasts
    • E. Kotera, M. Tasaka, and T. Shikanai A pentatricopetide repeat protein is essential for RNA editing in chloroplasts Nature 433 2005 326 330
    • (2005) Nature , vol.433 , pp. 326-330
    • Kotera, E.1    Tasaka, M.2    Shikanai, T.3
  • 9
    • 0025577587 scopus 로고
    • RNA editing of wheat mitochondrial ATP synthase subunit 9: direct protein and cDNA sequencing
    • D. Bégu, P.V. Graves, C. Domec, G. Arselin, S. Litvak, and A. Araya RNA editing of wheat mitochondrial ATP synthase subunit 9: direct protein and cDNA sequencing Plant Cell 2 1990 1283 1290
    • (1990) Plant Cell , vol.2 , pp. 1283-1290
    • Bégu, D.1    Graves, P.V.2    Domec, C.3    Arselin, G.4    Litvak, S.5    Araya, A.6
  • 10
    • 79957886185 scopus 로고    scopus 로고
    • The evolution of RNA editing and pentatricopeptide repeat genes
    • S. Fujii, and I. Small The evolution of RNA editing and pentatricopeptide repeat genes New Phytol. 191 2011 37 47
    • (2011) New Phytol. , vol.191 , pp. 37-47
    • Fujii, S.1    Small, I.2
  • 11
    • 84899745039 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins in plants
    • A. Barkan, and I. Small Pentatricopeptide repeat proteins in plants Annu. Rev. Plant Biol. 65 2014 415 442
    • (2014) Annu. Rev. Plant Biol. , vol.65 , pp. 415-442
    • Barkan, A.1    Small, I.2
  • 12
    • 84863957655 scopus 로고    scopus 로고
    • Mechanistic insight into pentatricopeptide repeat proteins as sequence-specific RNA-binding proteins for organellar RNAs in plants
    • T. Nakamura, Y. Yagi, and K. Kobayashi Mechanistic insight into pentatricopeptide repeat proteins as sequence-specific RNA-binding proteins for organellar RNAs in plants Plant Cell Physiol. 53 2012 1171 1179
    • (2012) Plant Cell Physiol. , vol.53 , pp. 1171-1179
    • Nakamura, T.1    Yagi, Y.2    Kobayashi, K.3
  • 13
    • 56549095978 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins: a socket set for organelle gene expression
    • C. Schmitz-Linneweber, and I. Small Pentatricopeptide repeat proteins: a socket set for organelle gene expression Trends Plant Sci. 13 2008 663 670
    • (2008) Trends Plant Sci. , vol.13 , pp. 663-670
    • Schmitz-Linneweber, C.1    Small, I.2
  • 14
    • 33645074681 scopus 로고    scopus 로고
    • RNA editing in plant organelles: machinery, physiological function and evolution
    • T. Shikanai RNA editing in plant organelles: machinery, physiological function and evolution Cell. Mol. Life Sci. 63 2006 698 708
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 698-708
    • Shikanai, T.1
  • 15
    • 84885171267 scopus 로고    scopus 로고
    • Why do plants edit RNA in plant organelles?
    • C.E. Bullerwell, Springer-Verlag Berlin Heidelberg
    • T. Shikanai Why do plants edit RNA in plant organelles? C.E. Bullerwell, Organelle Genetics 2012 Springer-Verlag Berlin Heidelberg
    • (2012) Organelle Genetics
    • Shikanai, T.1
  • 16
    • 84885171179 scopus 로고    scopus 로고
    • Function of PPR proteins in plastid gene expression
    • T. Shikanai, and S. Fujii Function of PPR proteins in plastid gene expression RNA Biol. 10 2013 31 41
    • (2013) RNA Biol. , vol.10 , pp. 31-41
    • Shikanai, T.1    Fujii, S.2
  • 17
    • 0029989864 scopus 로고    scopus 로고
    • Sequences directing C to U editing of the plastid psbL mRNA are located within a 22 nucleotide segment spanning the editing site
    • S. Chaudhuri, and P. Maliga Sequences directing C to U editing of the plastid psbL mRNA are located within a 22 nucleotide segment spanning the editing site EMBO J. 15 1996 5958 5964
    • (1996) EMBO J. , vol.15 , pp. 5958-5964
    • Chaudhuri, S.1    Maliga, P.2
  • 18
    • 0035282916 scopus 로고    scopus 로고
    • Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: development of a chloroplast in vitro RNA editing system
    • T. Hirose, and M. Sugiura Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: development of a chloroplast in vitro RNA editing system EMBO J. 20 2001 1144 1152
    • (2001) EMBO J. , vol.20 , pp. 1144-1152
    • Hirose, T.1    Sugiura, M.2
  • 21
    • 33845986746 scopus 로고    scopus 로고
    • A pentatricopeptide repeat protein is a site recognition factor in chloroplast RNA editing
    • K. Okuda, T. Nakamura, M. Sugita, T. Shimizu, and T. Shikanai A pentatricopeptide repeat protein is a site recognition factor in chloroplast RNA editing J. Biol. Chem. 281 2006 37661 37667
    • (2006) J. Biol. Chem. , vol.281 , pp. 37661-37667
    • Okuda, K.1    Nakamura, T.2    Sugita, M.3    Shimizu, T.4    Shikanai, T.5
  • 23
    • 67651171227 scopus 로고    scopus 로고
    • Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts
    • J. Pfalz, O.A. Bayraktar, J. Prikryl, and A. Barkan Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts EMBO J. 28 2009 2042 2052
    • (2009) EMBO J. , vol.28 , pp. 2042-2052
    • Pfalz, J.1    Bayraktar, O.A.2    Prikryl, J.3    Barkan, A.4
  • 24
    • 78651068887 scopus 로고    scopus 로고
    • Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein
    • J. Prikryl, M. Rojas, G. Schuster, and A. Barkan Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein Proc. Natl. Acad. Sci. U. S. A. 108 2011 415 420
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 415-420
    • Prikryl, J.1    Rojas, M.2    Schuster, G.3    Barkan, A.4
  • 25
    • 84860153569 scopus 로고    scopus 로고
    • Protein-mediated protection as the predominant mechanism for defining processed mRNA termini in land plant chloroplasts
    • R. Zhelyazkova, K. Hammani, M. Rojas, R. Voelker, M. Vargas-Suárez, T. Börner, and A. Barkan Protein-mediated protection as the predominant mechanism for defining processed mRNA termini in land plant chloroplasts Nucleic Acids Res. 40 2012 3092 3105
    • (2012) Nucleic Acids Res. , vol.40 , pp. 3092-3105
    • Zhelyazkova, R.1    Hammani, K.2    Rojas, M.3    Voelker, R.4    Vargas-Suárez, M.5    Börner, T.6    Barkan, A.7
  • 26
    • 84860147226 scopus 로고    scopus 로고
    • Short non-coding RNA fragments accumulating in chloroplasts: footprints of RNA binding proteins?
    • H. Ruwe, and C. Schmitz-Linneweber Short non-coding RNA fragments accumulating in chloroplasts: footprints of RNA binding proteins? Nucleic Acids Res. 40 2012 3106 3116
    • (2012) Nucleic Acids Res. , vol.40 , pp. 3106-3116
    • Ruwe, H.1    Schmitz-Linneweber, C.2
  • 27
    • 1842483066 scopus 로고    scopus 로고
    • PPR motifs of the nucleus-encoded factor, PGR3, function in the selective and distinct steps of chloroplast gene expression in Arabidopsis
    • H. Yamazaki, M. Tasaka, and T. Shikanai PPR motifs of the nucleus-encoded factor, PGR3, function in the selective and distinct steps of chloroplast gene expression in Arabidopsis Plant J. 38 2004 152 163
    • (2004) Plant J. , vol.38 , pp. 152-163
    • Yamazaki, H.1    Tasaka, M.2    Shikanai, T.3
  • 28
    • 79960208588 scopus 로고    scopus 로고
    • Proton gradient regulation 3 recognizes multiple targets with limited similarity and mediates translation and RNA stabilization in plastids
    • W. Cai, K. Okuda, L. Peng, and T. Shikanai Proton gradient regulation 3 recognizes multiple targets with limited similarity and mediates translation and RNA stabilization in plastids Plant J. 67 2011 318 327
    • (2011) Plant J. , vol.67 , pp. 318-327
    • Cai, W.1    Okuda, K.2    Peng, L.3    Shikanai, T.4
  • 29
    • 84884686240 scopus 로고    scopus 로고
    • Modulation of the RNA-binding activity of individual PPR motifs reveals the functional partitioning of proton gradient regulation 3
    • S. Fujii, N. Sato, and T. Shikanai Modulation of the RNA-binding activity of individual PPR motifs reveals the functional partitioning of proton gradient regulation 3 Plant Cell 25 2013 3079 3088
    • (2013) Plant Cell , vol.25 , pp. 3079-3088
    • Fujii, S.1    Sato, N.2    Shikanai, T.3
  • 30
    • 0345393082 scopus 로고    scopus 로고
    • A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis
    • M. Hashimoto, T. Endo, G. Peltier, M. Tasaka, and T. Shikanai A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis Plant J. 36 2003 541 549
    • (2003) Plant J. , vol.36 , pp. 541-549
    • Hashimoto, M.1    Endo, T.2    Peltier, G.3    Tasaka, M.4    Shikanai, T.5
  • 31
    • 57149118430 scopus 로고    scopus 로고
    • A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity
    • T. Nakamura, and M. Sugita A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity FEBS Lett. 582 2008 4163 4168
    • (2008) FEBS Lett. , vol.582 , pp. 4163-4168
    • Nakamura, T.1    Sugita, M.2
  • 32
    • 84859495332 scopus 로고    scopus 로고
    • A PPR-DYW protein is required for splicing of a group II intron of cox1 pre-mRNA in Physcomitrella patens
    • M. Ichinose, E. Tasaki, C. Sugita, and M. Sugita A PPR-DYW protein is required for splicing of a group II intron of cox1 pre-mRNA in Physcomitrella patens Plant J. 70 2012 271 278
    • (2012) Plant J. , vol.70 , pp. 271-278
    • Ichinose, M.1    Tasaki, E.2    Sugita, C.3    Sugita, M.4
  • 33
    • 84866145891 scopus 로고    scopus 로고
    • A combinatorial amino acid code for RNA recognition by pentatricopeptide repeat proteins
    • A. Barkan, M. Rojas, S. Fujii, A. Yap, Y.S. Chong, C.S. Bond, and I. Small A combinatorial amino acid code for RNA recognition by pentatricopeptide repeat proteins PLoS Genet. 8 2012 e1002910
    • (2012) PLoS Genet. , vol.8
    • Barkan, A.1    Rojas, M.2    Fujii, S.3    Yap, A.4    Chong, Y.S.5    Bond, C.S.6    Small, I.7
  • 34
  • 35
    • 84878784240 scopus 로고    scopus 로고
    • Improved computational target site prediction for pentatricopeptide repeat RNA editing factors
    • M. Takenaka, A. Zehrmann, A. Brennicke, and K. Graichen Improved computational target site prediction for pentatricopeptide repeat RNA editing factors PLoS ONE 8 2013 e65343
    • (2013) PLoS ONE , vol.8
    • Takenaka, M.1    Zehrmann, A.2    Brennicke, A.3    Graichen, K.4
  • 36
    • 79952166885 scopus 로고    scopus 로고
    • Selection patterns on restorer-like genes reveal a conflict between nuclear and mitochondrial genomes throughout angiosperm evolution
    • S. Fujii, C.S. Bond, and I.D. Small Selection patterns on restorer-like genes reveal a conflict between nuclear and mitochondrial genomes throughout angiosperm evolution Proc. Natl. Acad. Sci. U. S. A. 108 2011 1723 1728
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 1723-1728
    • Fujii, S.1    Bond, C.S.2    Small, I.D.3
  • 37
    • 84874588115 scopus 로고    scopus 로고
    • Elucidation of the RNA recognition code for pentatricopeptide repeat proteins involved in organelle RNA editing in plants
    • Y. Yagi, S. Hayashi, K. Kobayashi, T. Hirayama, and T. Nakamura Elucidation of the RNA recognition code for pentatricopeptide repeat proteins involved in organelle RNA editing in plants PLoS ONE 8 2013 e57286
    • (2013) PLoS ONE , vol.8
    • Yagi, Y.1    Hayashi, S.2    Kobayashi, K.3    Hirayama, T.4    Nakamura, T.5
  • 39
    • 84909594478 scopus 로고    scopus 로고
    • Examination of the dimerization states of the single-stranded RNA recognition protein pentatricopeptide repeat 10 (PPR10)
    • Q. Li, C. Yan, H. Xu, Z. Wang, J. Long, W. Li, J. Wu, P. Yin, and N. Yan Examination of the dimerization states of the single-stranded RNA recognition protein pentatricopeptide repeat 10 (PPR10) J. Biol. Chem. 289 2014 31503 31512
    • (2014) J. Biol. Chem. , vol.289 , pp. 31503-31512
    • Li, Q.1    Yan, C.2    Xu, H.3    Wang, Z.4    Long, J.5    Li, W.6    Wu, J.7    Yin, P.8    Yan, N.9
  • 40
    • 0038457836 scopus 로고    scopus 로고
    • HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs
    • K. Meierhoff, S. Felder, T. Nakamura, N. Bechtold, and G. Schuster HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs Plant Cell 15 2003 1480 1495
    • (2003) Plant Cell , vol.15 , pp. 1480-1495
    • Meierhoff, K.1    Felder, S.2    Nakamura, T.3    Bechtold, N.4    Schuster, G.5
  • 43
    • 73249140998 scopus 로고    scopus 로고
    • General features of chloroplast RNA editing factors and their target sites gained from a study of new Arabidopsis editing mutants
    • K. Hammani, K. Okuda, S. Tanz, A.L. Chategner-Boutin, T. Shikanai, and I. Small General features of chloroplast RNA editing factors and their target sites gained from a study of new Arabidopsis editing mutants Plant Cell 21 2009 3686 3699
    • (2009) Plant Cell , vol.21 , pp. 3686-3699
    • Hammani, K.1    Okuda, K.2    Tanz, S.3    Chategner-Boutin, A.L.4    Shikanai, T.5    Small, I.6
  • 44
    • 84862224565 scopus 로고    scopus 로고
    • A pentatricopeptide repeat protein acts as a site-specificity factor at multiple RNA editing sites with unrelated cis-acting elements in plastids
    • K. Okuda, and T. Shikanai A pentatricopeptide repeat protein acts as a site-specificity factor at multiple RNA editing sites with unrelated cis-acting elements in plastids Nucleic Acids Res. 40 2012 5052 5064
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5052-5064
    • Okuda, K.1    Shikanai, T.2
  • 45
    • 84859475178 scopus 로고    scopus 로고
    • Multiple organellar RNA editing factor (MORF) family proteins are required for RNA editing in mitochondria and plastids of plants
    • M. Takenaka, A. Zehrmann, D. Verbitskiy, M. Kugelmann, B. Härtel, and A. Brennicke Multiple organellar RNA editing factor (MORF) family proteins are required for RNA editing in mitochondria and plastids of plants Proc. Natl. Acad. Sci. U. S. A. 109 2012 5104 5109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5104-5109
    • Takenaka, M.1    Zehrmann, A.2    Verbitskiy, D.3    Kugelmann, M.4    Härtel, B.5    Brennicke, A.6
  • 47
    • 84879678855 scopus 로고    scopus 로고
    • Comprehensive high-resolution analysis of the role of an Arabidopsis gene family in RNA editing
    • S. Bentolila, J. Oh, M.R. Hanson, and R. Bukowski Comprehensive high-resolution analysis of the role of an Arabidopsis gene family in RNA editing PLoS Genet. 9 2013 e1003584
    • (2013) PLoS Genet. , vol.9
    • Bentolila, S.1    Oh, J.2    Hanson, M.R.3    Bukowski, R.4
  • 52
    • 84890952588 scopus 로고    scopus 로고
    • Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains
    • M.L. Hayes, K. Giang, B. Berhane, and R.M. Mulligan Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains J. Biol. Chem. 288 2013 36519 36529
    • (2013) J. Biol. Chem. , vol.288 , pp. 36519-36529
    • Hayes, M.L.1    Giang, K.2    Berhane, B.3    Mulligan, R.M.4
  • 54
    • 84924337180 scopus 로고    scopus 로고
    • Quantitative analysis of motifs contributing to the interaction between PLS-subfamily members and their target RNA sequences in plastid RNA editing
    • K. Okuda, H. Shoki, M. Arai, T. Shikanai, I. Small, and T. Nakamura Quantitative analysis of motifs contributing to the interaction between PLS-subfamily members and their target RNA sequences in plastid RNA editing Plant J. 2014 10.1111/tpj.12687
    • (2014) Plant J.
    • Okuda, K.1    Shoki, H.2    Arai, M.3    Shikanai, T.4    Small, I.5    Nakamura, T.6
  • 56
    • 77957167782 scopus 로고    scopus 로고
    • RNA editing competence of trans-factor MEF1 is modulated by ecotype-specific differences but requires the DYW domain
    • A. Zehrmann, D. Verbitskiy, B. Härtel, A. Brennicke, and M. Takenaka RNA editing competence of trans-factor MEF1 is modulated by ecotype-specific differences but requires the DYW domain FEBS Lett. 584 2010 4181 4186
    • (2010) FEBS Lett. , vol.584 , pp. 4181-4186
    • Zehrmann, A.1    Verbitskiy, D.2    Härtel, B.3    Brennicke, A.4    Takenaka, M.5
  • 57
    • 0030729775 scopus 로고    scopus 로고
    • Both RNA editing and RNA cleavage are required for translation of tobacco chloroplast ndhD mRNA: a possible regulatory mechanism for the expression of a chloroplast operon consisting of functionally unrelated genes
    • T. Hirose, and M. Sugiura Both RNA editing and RNA cleavage are required for translation of tobacco chloroplast ndhD mRNA: a possible regulatory mechanism for the expression of a chloroplast operon consisting of functionally unrelated genes EMBO J. 16 1997 6804 6811
    • (1997) EMBO J. , vol.16 , pp. 6804-6811
    • Hirose, T.1    Sugiura, M.2
  • 58
    • 56049116911 scopus 로고    scopus 로고
    • Amino acid sequence variations in Nicotiana CRR4 orthologs determine the species-specific efficiency of RNA editing in plastids
    • K. Okuda, Y. Habata, Y. Kobayashi, and T. Shikanai Amino acid sequence variations in Nicotiana CRR4 orthologs determine the species-specific efficiency of RNA editing in plastids Nucleic Acids Res. 36 2008 6155 6164
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6155-6164
    • Okuda, K.1    Habata, Y.2    Kobayashi, Y.3    Shikanai, T.4
  • 59
    • 80052879596 scopus 로고    scopus 로고
    • Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature for nuclear-encoded subunits
    • K. Ifuku, T. Endo, T. Shikanai, and E.M. Aro Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature for nuclear-encoded subunits Plant Cell Physiol. 52 2011 1560 1568
    • (2011) Plant Cell Physiol. , vol.52 , pp. 1560-1568
    • Ifuku, K.1    Endo, T.2    Shikanai, T.3    Aro, E.M.4
  • 60
    • 79957773110 scopus 로고    scopus 로고
    • An Src homology 3 domain-like fold protein forms a ferredoxin binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • H. Yamamoto, L. Peng, Y. Fukao, and T. Shikanai An Src homology 3 domain-like fold protein forms a ferredoxin binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis Plant Cell 23 2011 1480 1493
    • (2011) Plant Cell , vol.23 , pp. 1480-1493
    • Yamamoto, H.1    Peng, L.2    Fukao, Y.3    Shikanai, T.4
  • 62
    • 73249123281 scopus 로고    scopus 로고
    • Efficient operation of NAD(P)H dehydrogenase requires supercomplex formation with photosystem I via minor LHCI in Arabidopsis
    • L. Peng, Y. Fukao, M. Fujiwara, T. Takami, and T. Shikanai Efficient operation of NAD(P)H dehydrogenase requires supercomplex formation with photosystem I via minor LHCI in Arabidopsis Plant Cell 21 2009 3623 3640
    • (2009) Plant Cell , vol.21 , pp. 3623-3640
    • Peng, L.1    Fukao, Y.2    Fujiwara, M.3    Takami, T.4    Shikanai, T.5
  • 63
    • 84868456486 scopus 로고    scopus 로고
    • Composition and physiological function of the chloroplast NADH dehydrogenase-like complex in Marchantia polymorpha
    • M. Ueda, T. Kuniyoshi, H. Yamamoto, K. Sugimoto, K. Ishizaki, T. Kohchi, Y. Nishimura, and T. Shikanai Composition and physiological function of the chloroplast NADH dehydrogenase-like complex in Marchantia polymorpha Plant J. 72 2012 683 693
    • (2012) Plant J. , vol.72 , pp. 683-693
    • Ueda, M.1    Kuniyoshi, T.2    Yamamoto, H.3    Sugimoto, K.4    Ishizaki, K.5    Kohchi, T.6    Nishimura, Y.7    Shikanai, T.8
  • 64
    • 58049211385 scopus 로고    scopus 로고
    • The chloroplast NAD(P)H dehydrogenase complex interacts with photosystem I in Arabidopsis
    • L. Peng, H. Shimizu, and T. Shikanai The chloroplast NAD(P)H dehydrogenase complex interacts with photosystem I in Arabidopsis J. Biol. Chem. 283 2008 34873 34879
    • (2008) J. Biol. Chem. , vol.283 , pp. 34873-34879
    • Peng, L.1    Shimizu, H.2    Shikanai, T.3
  • 65
    • 79953681329 scopus 로고    scopus 로고
    • Supercomplex formation with photosystem I is required for the stabilization of the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • L. Peng, and T. Shikanai Supercomplex formation with photosystem I is required for the stabilization of the chloroplast NADH dehydrogenase-like complex in Arabidopsis Plant Physiol. 155 2011 1629 1639
    • (2011) Plant Physiol. , vol.155 , pp. 1629-1639
    • Peng, L.1    Shikanai, T.2
  • 66
    • 79958120495 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: novel insights and remaining puzzles
    • N. Battchikova, M. Eisenhut, and E.M. Aro Cyanobacterial NDH-1 complexes: novel insights and remaining puzzles Biochim. Biophys. Acta 1807 2011 935 944
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 935-944
    • Battchikova, N.1    Eisenhut, M.2    Aro, E.M.3
  • 67
    • 84901620558 scopus 로고    scopus 로고
    • The potential for manipulating RNA with pentatricopeptide repeat proteins
    • Y. Yagi, T. Nakamura, and I. Small The potential for manipulating RNA with pentatricopeptide repeat proteins Plant J. 78 2014 772 782
    • (2014) Plant J. , vol.78 , pp. 772-782
    • Yagi, Y.1    Nakamura, T.2    Small, I.3


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