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Volumn 235, Issue 1-2, 1999, Pages 131-137

The mitochondrial Pylaiella littoralis nad11 gene contains only the N-terminal FeS-binding domain

Author keywords

Brown algae; Complex I; NADH:ubiquinone oxidoreductase; nuo and hoxU genes

Indexed keywords

MITOCHONDRIAL DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 0032790881     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00194-8     Document Type: Article
Times cited : (8)

References (26)
  • 1
    • 0024698307 scopus 로고
    • Translational regulation of the lysis gene in RNA bacteriophage fr requires a UUG initiation codon
    • Adhin M.R., van Duin J. Translational regulation of the lysis gene in RNA bacteriophage fr requires a UUG initiation codon. Mol. Gen. Genet. 218:1989;137-142.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 137-142
    • Adhin, M.R.1    Van Duin, J.2
  • 3
    • 0030571582 scopus 로고    scopus 로고
    • Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechococcus sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P) H-dehydrogenase (complex I)
    • Appel J., Schulz R. Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechococcus sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P) H-dehydrogenase (complex I). Biochim. Biophys. Acta. 1298:1996;141-147.
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 141-147
    • Appel, J.1    Schulz, R.2
  • 4
    • 0030607245 scopus 로고    scopus 로고
    • Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans
    • Boison G., Schmitz L., Mikheeva L., Shestakov S., Bothe H. Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans. FEBS Lett. 394:1996;153-158.
    • (1996) FEBS Lett. , vol.394 , pp. 153-158
    • Boison, G.1    Schmitz, L.2    Mikheeva, L.3    Shestakov, S.4    Bothe, H.5
  • 5
    • 0032490101 scopus 로고    scopus 로고
    • Organization and evolution of structural elements within complex I
    • Finel M. Organization and evolution of structural elements within complex I. Biochim. Biophys. Acta. 1364:1998;112-121.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 112-121
    • Finel, M.1
  • 6
    • 0029113811 scopus 로고
    • The mitochondrial LSU rDNA of the brown alga Pylaiella littoralis reveals α-proteobacterial features and is split by four group IIB introns with an atypical phylogeny
    • Fontaine J.-M., Rousvoal S., Leblanc C., Kloareg B., Loiseaux-de Goër S. The mitochondrial LSU rDNA of the brown alga Pylaiella littoralis reveals α-proteobacterial features and is split by four group IIB introns with an atypical phylogeny. J. Mol. Biol. 251:1995;378-389.
    • (1995) J. Mol. Biol. , vol.251 , pp. 378-389
    • Fontaine, J.-M.1    Rousvoal, S.2    Leblanc, C.3    Kloareg, B.4    Loiseaux-De Goër, S.5
  • 8
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54:1985;1015-1069.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 9
    • 0030905348 scopus 로고    scopus 로고
    • Protein and gene structure of the NADH-binding fragment of Rhodobacter capsulatus NADH : Ubiquinone oxidoreductase
    • Herter S.M., Schiltz E., Drews G. Protein and gene structure of the NADH-binding fragment of Rhodobacter capsulatus NADH : ubiquinone oxidoreductase. Eur. J. Biochem. 246:1997;800-808.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 800-808
    • Herter, S.M.1    Schiltz, E.2    Drews, G.3
  • 10
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1
  • 11
    • 0024295214 scopus 로고    scopus 로고
    • Effect of structure of the initiator codon on translation in E. coli
    • Khudyakov Yu.E., Neplyueva V.S., Kalinina T.I., Smirnov V.D. Effect of structure of the initiator codon on translation in E. coli. FEBS Lett. 232:1998;369-371.
    • (1998) FEBS Lett. , vol.232 , pp. 369-371
    • Khudyakov, Yu.E.1    Neplyueva, V.S.2    Kalinina, T.I.3    Smirnov, V.D.4
  • 12
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH:ubiquinone oxydoreductase from Escherichia coli
    • Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T. Isolation and characterization of the proton-translocating NADH:ubiquinone oxydoreductase from Escherichia coli. Eur. J. Biochem. 230:1995;538-548.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 13
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki S., Saimmaime I., de Luca G., Rousset M., Dermoun Z., Belaich J.-P. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bact. 177:1995;2628-2636.
    • (1995) J. Bact. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.-P.6
  • 14
    • 0025886958 scopus 로고
    • Primary structures of two subunits of NADH: Ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.A., van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H. Primary structures of two subunits of NADH: ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus. Biochim. Biophys. Acta. 1090:1991;133-138.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 133-138
    • Preis, D.1    Weidner, U.2    Conzen, C.3    Azevedo, J.E.4    Nehls, U.5    Roehlen, D.A.6    Van Der Pas, J.C.7    Sackmann, U.8    Schneider, R.9    Werner, S.10    Weiss, H.11
  • 15
    • 0032053605 scopus 로고    scopus 로고
    • Molecular characterisation of the 76 kDa iron-sulphur protein subunit of potato mitochondrial Complex I
    • Rasmusson A.G., Heiser V., Irrgang K.D., Brennicke A., Grohmann L. Molecular characterisation of the 76 kDa iron-sulphur protein subunit of potato mitochondrial Complex I. Plant Cell Physiol. 39:1998;373-381.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 373-381
    • Rasmusson, A.G.1    Heiser, V.2    Irrgang, K.D.3    Brennicke, A.4    Grohmann, L.5
  • 16
    • 0032540298 scopus 로고    scopus 로고
    • Witnessing the evolution of transcription in mitochondria: The mitochondrial genome of the primitive brown alga Pylaiella littoralis (L.) Kjellm. encodes a T7-like RNA polymerase
    • Rousvoal S., Oudot M.-P., Fontaine J.-M., Kloareg B., Loiseaux-de Goër S. Witnessing the evolution of transcription in mitochondria: the mitochondrial genome of the primitive brown alga Pylaiella littoralis (L.) Kjellm. encodes a T7-like RNA polymerase. J. Mol. Biol. 277:1998;1047-1057.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1047-1057
    • Rousvoal, S.1    Oudot, M.-P.2    Fontaine, J.-M.3    Kloareg, B.4    Loiseaux-De Goër, S.5
  • 17
    • 0024350374 scopus 로고
    • Mitochondrial NADH:ubiquinone reductase: Complementary DNA sequence of the import precursor of the bovine 75-kDa subunit
    • Runswick M.J., Gennis R.B., Fearnley I.M., Walker J.E. Mitochondrial NADH:ubiquinone reductase: complementary DNA sequence of the import precursor of the bovine 75-kDa subunit. Biochimie. 28:1989;9452-9459.
    • (1989) Biochimie , vol.28 , pp. 9452-9459
    • Runswick, M.J.1    Gennis, R.B.2    Fearnley, I.M.3    Walker, J.E.4
  • 19
    • 0032551756 scopus 로고    scopus 로고
    • A phylogenetic analysis of the cytochrome b and cytochrome c oxidase I genes supports an origin of mitochondria from within the Rickettsiaceae
    • Sicheritz-Pontén T., Kurland G., Andersson S.G.E. A phylogenetic analysis of the cytochrome b and cytochrome c oxidase I genes supports an origin of mitochondria from within the Rickettsiaceae. Biochim. Biophys. Acta. 1365:1998;545-551.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 545-551
    • Sicheritz-Pontén, T.1    Kurland, G.2    Andersson, S.G.E.3
  • 20
    • 0024391852 scopus 로고
    • Translational reinitiation in the presence and absence of a Shine and Dalgarno sequence
    • Spanjaard R.A., van Duin J. Translational reinitiation in the presence and absence of a Shine and Dalgarno sequence. Nucleic Acids Res. 17:1989;5501-5507.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5501-5507
    • Spanjaard, R.A.1    Van Duin, J.2
  • 21
    • 0024655902 scopus 로고
    • Hyd-γ, a gene from Desulfovibrio vulgaris (Hildenborough) encodes a polypeptide homologous to the periplasmic hydrogenase
    • Stokkermans J., van Dongen W., Kaan A., van den Berg W., Veeger C. Hyd-γ, a gene from Desulfovibrio vulgaris (Hildenborough) encodes a polypeptide homologous to the periplasmic hydrogenase. FEMS Microbiol. Lett. 58:1989;217-222.
    • (1989) FEMS Microbiol. Lett. , vol.58 , pp. 217-222
    • Stokkermans, J.1    Van Dongen, W.2    Kaan, A.3    Van Den Berg, W.4    Veeger, C.5
  • 22
    • 0025291627 scopus 로고
    • Cloning and nucleotide sequence of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
    • Tran-Betcke A., Warnecke U., Böcker C., Zaborosch C., Friedrich B. Cloning and nucleotide sequence of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 172:1990;2920-2929.
    • (1990) J. Bacteriol. , vol.172 , pp. 2920-2929
    • Tran-Betcke, A.1    Warnecke, U.2    Böcker, C.3    Zaborosch, C.4    Friedrich, B.5
  • 23
    • 0028323420 scopus 로고
    • The chaperone connection to the origins of the eukaryotic organelles
    • Viale A.M., Arakaki A.K. The chaperone connection to the origins of the eukaryotic organelles. FEBS Lett. 341:1994;146-151.
    • (1994) FEBS Lett. , vol.341 , pp. 146-151
    • Viale, A.M.1    Arakaki, A.K.2
  • 24
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH : Ubiquinone oxidoreductase in Escherichia coli
    • Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. The gene locus of the proton-translocating NADH : ubiquinone oxidoreductase in Escherichia coli. J. Mol. Biol. 233:1993;109-122.
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 25
    • 0026634739 scopus 로고
    • Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans
    • Xu X., Matsuno-Yagi A., Yagi T. Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Arch. Biochem. Biophys. 296:1992;40-48.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 40-48
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.