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Volumn 162, Issue 2, 2013, Pages 581-588

Identification of mitochondrial coenzyme a transporters from maize and Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; EUDICOTYLEDONS; LILIOPSIDA; MAGNOLIOPHYTA; MAMMALIA; NICOTIANA TABACUM; PISUM SATIVUM; SACCHAROMYCES CEREVISIAE; ZEA MAYS;

EID: 84878441922     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.113.218081     Document Type: Article
Times cited : (32)

References (39)
  • 3
    • 0033963089 scopus 로고    scopus 로고
    • The ENZYME database in 2000
    • Bairoch A (2000) The ENZYME database in 2000. Nucleic Acids Res 28: 304-305
    • (2000) Nucleic Acids Res , vol.28 , pp. 304-305
    • Bairoch, A.1
  • 4
    • 27144449733 scopus 로고    scopus 로고
    • Folate metabolism in plants: An Arabi-dopsis homolog of the mammalian mitochondrial folate transporter mediates folate import into chloroplasts
    • Bedhomme M, Hoffmann M, McCarthy EA, Gambonnet B, Moran RG, Rébeillé F, Ravanel S (2005) Folate metabolism in plants: an Arabi-dopsis homolog of the mammalian mitochondrial folate transporter mediates folate import into chloroplasts. J Biol Chem 280: 34823-34831
    • (2005) J Biol Chem , vol.280 , pp. 34823-34831
    • Bedhomme, M.1    Hoffmann, M.2    McCarthy, E.A.3    Gambonnet, B.4    Moran, R.G.5    Rébeillé, F.6    Ravanel, S.7
  • 5
    • 84355162914 scopus 로고    scopus 로고
    • + and contributes to optimal fatty acid degradation during storage oil mobilization
    • + and contributes to optimal fatty acid degradation during storage oil mobilization. Plant J 69: 1-13
    • (2012) Plant J , vol.69 , pp. 1-13
    • Bernhardt, K.1    Wilkinson, S.2    Weber, A.P.3    Linka, N.4
  • 8
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria: Cytochrome b2 and cytochrome c peroxidase are located in the inter-membrane space of yeast mitochondria
    • Daum G, Böhni PC, Schatz G (1982) Import of proteins into mitochondria: cytochrome b2 and cytochrome c peroxidase are located in the inter-membrane space of yeast mitochondria. J Biol Chem 257: 13028-13033
    • (1982) J Biol Chem , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 11
    • 67650561215 scopus 로고    scopus 로고
    • A novel member of solute carrier family 25 (SLC25A42) is a transporter of coenzyme A and adenosine 39,59-diphosphate in human mitochondria
    • Fiermonte G, Paradies E, Todisco S, Marobbio CM, Palmieri F (2009) A novel member of solute carrier family 25 (SLC25A42) is a transporter of coenzyme A and adenosine 39,59-diphosphate in human mitochondria. J Biol Chem 284: 18152-18159
    • (2009) J Biol Chem , vol.284 , pp. 18152-18159
    • Fiermonte, G.1    Paradies, E.2    Todisco, S.3    Marobbio, C.M.4    Palmieri, F.5
  • 15
    • 0036138306 scopus 로고    scopus 로고
    • The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism
    • Hunt MC, Alexson SE (2002) The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res 41: 99-130
    • (2002) Prog Lipid Res , vol.41 , pp. 99-130
    • Hunt, M.C.1    Alexson, S.E.2
  • 16
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky O, Tawfik DS (2010) Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu Rev Biochem 79: 471-505
    • (2010) Annu Rev Biochem , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 17
    • 52649148626 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis Brittle1 transport protein and impact of reduced activity on plant metabolism
    • Kirchberger S, Tjaden J, Neuhaus HE (2008) Characterization of the Arabidopsis Brittle1 transport protein and impact of reduced activity on plant metabolism. Plant J 56: 51-63
    • (2008) Plant J , vol.56 , pp. 51-63
    • Kirchberger, S.1    Tjaden, J.2    Neuhaus, H.E.3
  • 19
    • 33645745752 scopus 로고    scopus 로고
    • The mitochondrial compartment
    • Logan DC (2006) The mitochondrial compartment. J Exp Bot 57: 1225-1243
    • (2006) J Exp Bot , vol.57 , pp. 1225-1243
    • Logan, D.C.1
  • 20
    • 0001321792 scopus 로고
    • Monoclonal antibodies to the a- and b-subunits of the plant mitochondrial F1-ATPase
    • Luethy MH, Horak A, Elthon TE (1993) Monoclonal antibodies to the a- and b-subunits of the plant mitochondrial F1-ATPase. Plant Physiol 101: 931-937
    • (1993) Plant Physiol , vol.101 , pp. 931-937
    • Luethy, M.H.1    Horak, A.2    Elthon, T.E.3
  • 21
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • Mannella CA (2006) Structure and dynamics of the mitochondrial inner membrane cristae. Biochim Biophys Acta 1763: 542-548
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 542-548
    • Mannella, C.A.1
  • 23
    • 38449110969 scopus 로고    scopus 로고
    • Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells
    • Miao Y, Jiang L (2007) Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells. Nat Protoc 2: 2348-2353
    • (2007) Nat Protoc , vol.2 , pp. 2348-2353
    • Miao, Y.1    Jiang, L.2
  • 24
  • 25
    • 84875218644 scopus 로고    scopus 로고
    • The mitochondrial transporter family SLC25: Identification, properties and physiopathology
    • Palmieri F (2013) The mitochondrial transporter family SLC25: identification, properties and physiopathology. Mol Aspects Med 34: 465-484
    • (2013) Mol Aspects Med , vol.34 , pp. 465-484
    • Palmieri, F.1
  • 26
    • 79953249623 scopus 로고    scopus 로고
    • Evolution, structure and function of mitochondrial carriers: A review with new insights
    • Palmieri F, Pierri CL, De Grassi A, Nunes-Nesi A, Fernie AR (2011) Evolution, structure and function of mitochondrial carriers: a review with new insights. Plant J 66: 161-181
    • (2011) Plant J , vol.66 , pp. 161-181
    • Palmieri, F.1    Pierri, C.L.2    de Grassi, A.3    Nunes-Nesi, A.4    Fernie, A.R.5
  • 28
    • 0032127892 scopus 로고    scopus 로고
    • Targeting and assembly of the oxoglutarate carrier: General principles for biogenesis of carrier proteins of the mitochondrial inner membrane
    • Palmisano A, Zara V, Hönlinger A, Vozza A, Dekker PJ, Pfanner N, Palmieri F (1998) Targeting and assembly of the oxoglutarate carrier: general principles for biogenesis of carrier proteins of the mitochondrial inner membrane. Biochem J 333: 151-158
    • (1998) Biochem J , vol.333 , pp. 151-158
    • Palmisano, A.1    Zara, V.2    Hönlinger, A.3    Vozza, A.4    Dekker, P.J.5    Pfanner, N.6    Palmieri, F.7
  • 29
    • 0035144432 scopus 로고    scopus 로고
    • The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix
    • Prohl C, Pelzer W, Diekert K, Kmita H, Bedekovics T, Kispal G, Lill R (2001) The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix. Mol Cell Biol 21: 1089-1097
    • (2001) Mol Cell Biol , vol.21 , pp. 1089-1097
    • Prohl, C.1    Pelzer, W.2    Diekert, K.3    Kmita, H.4    Bedekovics, T.5    Kispal, G.6    Lill, R.7
  • 30
    • 0035999898 scopus 로고    scopus 로고
    • A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts
    • Rudhe C, Chew O, Whelan J, Glaser E (2002) A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts. Plant J 30: 213-220
    • (2002) Plant J , vol.30 , pp. 213-220
    • Rudhe, C.1    Chew, O.2    Whelan, J.3    Glaser, E.4
  • 32
    • 61949403154 scopus 로고    scopus 로고
    • The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria
    • Suppanz IE, Wurm CA, Wenzel D, Jakobs S (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20: 572-580
    • (2009) Mol Biol Cell , vol.20 , pp. 572-580
    • Suppanz, I.E.1    Wurm, C.A.2    Wenzel, D.3    Jakobs, S.4
  • 33
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 34
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F (2002) Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3: RESEARCH0034
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    de Preter, K.2    Pattyn, F.3    Poppe, B.4    van Roy, N.5    de Paepe, A.6    Speleman, F.7
  • 35
    • 83855163237 scopus 로고    scopus 로고
    • Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron-sulphur cluster metabolism
    • Waller JC, Ellens KW, Alvarez S, Loizeau K, Ravanel S, Hanson AD (2012) Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron-sulphur cluster metabolism. J Exp Bot 63: 403-411
    • (2012) J Exp Bot , vol.63 , pp. 403-411
    • Waller, J.C.1    Ellens, K.W.2    Alvarez, S.3    Loizeau, K.4    Ravanel, S.5    Hanson, A.D.6
  • 36
    • 80051555494 scopus 로고    scopus 로고
    • Pantothenate biosynthesis in higher plants
    • Webb ME, Smith AG (2011) Pantothenate biosynthesis in higher plants. Adv Bot Res 58: 203-255
    • (2011) Adv Bot Res , vol.58 , pp. 203-255
    • Webb, M.E.1    Smith, A.G.2
  • 37
    • 40349091686 scopus 로고    scopus 로고
    • An "Electronic Fluorescent Pictograph" browser for exploring and analyzing large-scale biological data sets
    • Winter D, Vinegar B, Nahal H, Ammar R, Wilson GV, Provart NJ (2007) An "Electronic Fluorescent Pictograph" browser for exploring and analyzing large-scale biological data sets. PLoS ONE 2: e718
    • (2007) PLoS ONE , vol.2
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6
  • 38
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm CA, Jakobs S (2006) Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett 580: 5628-5634
    • (2006) FEBS Lett , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 39
    • 64249125928 scopus 로고    scopus 로고
    • Mitochondrial carrier protein biogenesis: Role of the chaperones Hsc70 and Hsp90
    • Zara V, Ferramosca A, Robitaille-Foucher P, Palmieri F, Young JC (2009) Mitochondrial carrier protein biogenesis: role of the chaperones Hsc70 and Hsp90. Biochem J 419: 369-375
    • (2009) Biochem J , vol.419 , pp. 369-375
    • Zara, V.1    Ferramosca, A.2    Robitaille-Foucher, P.3    Palmieri, F.4    Young, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.