메뉴 건너뛰기




Volumn 44, Issue 27, 2005, Pages 9545-9554

Characterization of the membrane domain subunit NuoK (ND4L) of the NADH-quinone oxidoreductase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; ELECTROPHORESIS; ESCHERICHIA COLI; GENES; PROTEINS;

EID: 21844440546     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050708w     Document Type: Article
Times cited : (57)

References (42)
  • 1
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
    • Yagi, T., and Matsuno-Yagi, A. (2003) The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked, Biochemistry 42, 2266-2214.
    • (2003) Biochemistry , vol.42 , pp. 2266-12214
    • Yagi, T.1    Matsuno-Yagi, A.2
  • 2
    • 0032588194 scopus 로고    scopus 로고
    • +/2e- Stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • +/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles, FEBS Lett. 451, 157-161.
    • (1999) FEBS Lett. , vol.451 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 3
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I: Identification of two new subunits
    • Carroll, J., Shannon, R. J., Fearnley, I. M., Walker, J. E., and Hirst, J. (2002) Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I: identification of two new subunits, J. Biol. Chem. 277, 50311-50317.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 6
    • 0038160473 scopus 로고    scopus 로고
    • Analysis of the subunit composition of complex I from bovine heart mitochondria
    • Carroll, J., Fearnley, I. M., Shannon, R. J., Hirst, J., and Walker, J. E. (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria, Mol. Cell. Proteomics 2, 117-126.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 117-126
    • Carroll, J.1    Fearnley, I.M.2    Shannon, R.J.3    Hirst, J.4    Walker, J.E.5
  • 7
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K., and Friedrich, T. (1998) Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I), J. Mol. Biol. 276, 105-112.
    • (1998) J. Mol. Biol. , vol.276 , pp. 105-112
    • Guénebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 8
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Friedrich, T. (1998) The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli, Biochim. Biophys. Acta 1364, 134-146.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 134-146
    • Friedrich, T.1
  • 9
    • 15844405973 scopus 로고    scopus 로고
    • Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Identity, property, and stoichiometry of the peripheral subunits
    • Takano, S., Yano, T., and Yagi, T. (1996) Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: identity, property, and stoichiometry of the peripheral subunits, Biochemistry 35, 9120-9127.
    • (1996) Biochemistry , vol.35 , pp. 9120-9127
    • Takano, S.1    Yano, T.2    Yagi, T.3
  • 10
    • 0033215393 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Studies on topology and stoichiometry of the peripheral subunits
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: studies on topology and stoichiometry of the peripheral subunits. J. Biol. Chem. 274, 28606-28611.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28606-28611
    • Yano, T.1    Yagi, T.2
  • 11
    • 0035941007 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase
    • +- translocating NADH-quinone oxidoreductase, FEBS Lett. 508, 385-388.
    • (2001) FEBS Lett. , vol.508 , pp. 385-388
    • Di Bernardo, S.1    Yagi, T.2
  • 12
    • 1642392110 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase probed by zero-length cross-linking
    • +-translocating NADH-quinone oxidoreductase probed by zero-length cross-linking, Biochemistry 43, 3750-3755.
    • (2004) Biochemistry , vol.43 , pp. 3750-3755
    • Kao, M.-C.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 13
    • 0033215197 scopus 로고    scopus 로고
    • Characterization of the putative 2x[4Fe-4S] binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Expression, reconstitution, and EPR characterization
    • Yano, T., Magnitsky, S., Sled', V. D., Ohnishi, T., and Yagi, T. (1999) Characterization of the putative 2x[4Fe-4S] binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: expression, reconstitution, and EPR characterization, J. Biol. Chem. 274, 28598-28605.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28598-28605
    • Yano, T.1    Magnitsky, S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 14
    • 0034622505 scopus 로고    scopus 로고
    • Exploring the membrane domain of the reduced nicotinamide adenine dinucleotide-quinone oxidoreductase of Paracoccus denitrificans: Characterization of the NQO7 subunit
    • Di Bernardo, S., Yano, T., and Yagi, T. (2000) Exploring the membrane domain of the reduced nicotinamide adenine dinucleotide-quinone oxidoreductase of Paracoccus denitrificans: characterization of the NQO7 subunit, Biochemistry 39, 9411-9418.
    • (2000) Biochemistry , vol.39 , pp. 9411-9418
    • Di Bernardo, S.1    Yano, T.2    Yagi, T.3
  • 15
    • 0037006973 scopus 로고    scopus 로고
    • Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Kao, M.-C., Di Bernardo, S., Matsuno-Yagi, A., and Yagi, T. (2002) Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, Biochemistry 41, 4377-4384.
    • (2002) Biochemistry , vol.41 , pp. 4377-4384
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 16
    • 0037461290 scopus 로고    scopus 로고
    • Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Kao, M.-C., Di Bernardo, S., Matsuno-Yagi, A., and Yagi, T. (2003) Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, Biochemistry 42, 4534-4543.
    • (2003) Biochemistry , vol.42 , pp. 4534-4543
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 17
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
    • Chomyn, A., Mariottini, P., Cleeter, M. W. J., Ragan, C. I., Matsuno-Yagi, A., Hatefi, Y., Doolittle, R. F., and Attardi, G. (1985) Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase, Nature 314, 591-597.
    • (1985) Nature , vol.314 , pp. 591-597
    • Chomyn, A.1    Mariottini, P.2    Cleeter, M.W.J.3    Ragan, C.I.4    Matsuno-Yagi, A.5    Hatefi, Y.6    Doolittle, R.F.7    Attardi, G.8
  • 18
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit
    • Chomyn, A., Cleeter, M. W. J., Ragan, C. I., Riley, M., Doolittle, R. F., and Attardi, G. (1986) URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit, Science 234, 614-618.
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.J.2    Ragan, C.I.3    Riley, M.4    Doolittle, R.F.5    Attardi, G.6
  • 19
    • 0347295939 scopus 로고    scopus 로고
    • The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I
    • Nakamaru-Ogiso, E., Sakamoto, K., Matsuno-Yagi, A., Miyoshi, H., and Yagi, T. (2003) The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I, Biochemistry 42, 746-754.
    • (2003) Biochemistry , vol.42 , pp. 746-754
    • Nakamaru-Ogiso, E.1    Sakamoto, K.2    Matsuno-Yagi, A.3    Miyoshi, H.4    Yagi, T.5
  • 20
    • 0037815067 scopus 로고    scopus 로고
    • The ubiquinone-binding site in NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Gong, X., Xie, T., Yu, L., Hesterberg, M., Scheide, D., Friedrich, T., and Yu, C. A. (2003) The ubiquinone-binding site in NADH: ubiquinone oxidoreductase from Escherichia coli, J. Biol. Chem. 278, 25731-25737.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25731-25737
    • Gong, X.1    Xie, T.2    Yu, L.3    Hesterberg, M.4    Scheide, D.5    Friedrich, T.6    Yu, C.A.7
  • 22
    • 0031970873 scopus 로고    scopus 로고
    • Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH-ubiquinone oxidoreductase
    • Dupuis, A., Darrouzet, E., Duborjal, H., Pierrard, B., Chevallet, M., Van Beizen, R., Albracht, S. P., and Lunardi, J. (1998) Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH-ubiquinone oxidoreductase, Mol. Microbiol. 28, 531-541.
    • (1998) Mol. Microbiol. , vol.28 , pp. 531-541
    • Dupuis, A.1    Darrouzet, E.2    Duborjal, H.3    Pierrard, B.4    Chevallet, M.5    Van Beizen, R.6    Albracht, S.P.7    Lunardi, J.8
  • 23
    • 0032490101 scopus 로고    scopus 로고
    • Organization and evolution of structural elements within complex I
    • Finel, M. (1998) Organization and evolution of structural elements within complex I, Biochim. Biophys. Acta 1364, 112-121.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 112-121
    • Finel, M.1
  • 24
    • 0041563699 scopus 로고    scopus 로고
    • The 'antiporter module' of respiratory chain complex I includes the MrpC/NuoK subunit - A revision of the modular evolution scheme
    • Mathiesen, C., and Hagerhall, C. (2003) The 'antiporter module' of respiratory chain complex I includes the MrpC/NuoK subunit-a revision of the modular evolution scheme, FEBS Lett. 549, 7-13.
    • (2003) FEBS Lett. , vol.549 , pp. 7-13
    • Mathiesen, C.1    Hagerhall, C.2
  • 25
    • 1642494896 scopus 로고    scopus 로고
    • A pair of membrane-embedded acidic residues in the NuoK subunit of Escherichia coli NDH-1, a counterpart of the ND4L subunit of the mitochondrial complex I, are required for high ubiquinone reductase activity
    • Kervinen, M., Patsi, J., Finel, M., and Hassinen, I. E. (2004) A pair of membrane-embedded acidic residues in the NuoK subunit of Escherichia coli NDH-1, a counterpart of the ND4L subunit of the mitochondrial complex I, are required for high ubiquinone reductase activity, Biochemistry 43, 773-781.
    • (2004) Biochemistry , vol.43 , pp. 773-781
    • Kervinen, M.1    Patsi, J.2    Finel, M.3    Hassinen, I.E.4
  • 26
    • 14644386835 scopus 로고    scopus 로고
    • Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation
    • Kao, M.-C., Di Bernardo, S., Nakamaru-Ogiso, E., Miyoshi, H., Matsuno-Yagi, A., and Yagi, T. (2005) Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation, Biochemistry 44, 3562-3571.
    • (2005) Biochemistry , vol.44 , pp. 3562-3571
    • Kao, M.-C.1    Di Bernardo, S.2    Nakamaru-Ogiso, E.3    Miyoshi, H.4    Matsuno-Yagi, A.5    Yagi, T.6
  • 27
    • 0022305933 scopus 로고
    • Transposon Tn554: Complete nucleotide sequence and isolation of transposition-defective and antibiotic-sensitive mutants
    • Murphy, E., Huwyler, L., and Freire Bastos, M. C. (1985) Transposon Tn554: complete nucleotide sequence and isolation of transposition-defective and antibiotic-sensitive mutants, EMBO J. 4, 3357-3365.
    • (1985) EMBO J. , vol.4 , pp. 3357-3365
    • Murphy, E.1    Huwyler, L.2    Freire Bastos, M.C.3
  • 28
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization
    • Link, A. J., Phillips, D., and Church, G. M. (1997) Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization, J. Bacteriol. 179, 6228-6237.
    • (1997) J. Bacteriol. , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 29
    • 3542993823 scopus 로고    scopus 로고
    • Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli
    • Kao, M.-C., Di Bernardo, S., Perego, M., Nakamaru-Ogiso, E., Matsuno-Yagi, A., and Yagi, T. (2004) Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli, J. Biol. Chem. 279, 32360-32366.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32360-32366
    • Kao, M.-C.1    Di Bernardo, S.2    Perego, M.3    Nakamaru-Ogiso, E.4    Matsuno-Yagi, A.5    Yagi, T.6
  • 30
    • 0024460744 scopus 로고
    • Studies on the structure of NADH:ubiquinone oxidoreductase complex: Topography of the subunits of the iron-sulfur protein component
    • Man, A.-L., Yagi, T., and Hatefi, Y. (1989) Studies on the structure of NADH:ubiquinone oxidoreductase complex: topography of the subunits of the iron-sulfur protein component, Arch. Biochem. Biophys. 275, 166-173.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 166-173
    • Man, A.-L.1    Yagi, T.2    Hatefi, Y.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H., and Von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form, Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 33
    • 0023463947 scopus 로고
    • NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
    • Matsushita, K., Ohnishi, T., and Kaback, H. R. (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain, Biochemistry 26, 7732-7737.
    • (1987) Biochemistry , vol.26 , pp. 7732-7737
    • Matsushita, K.1    Ohnishi, T.2    Kaback, H.R.3
  • 34
    • 0022974638 scopus 로고
    • Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans
    • Yagi, T. (1986) Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans, Arch. Biochem. Biophys. 250, 302-311.
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 302-311
    • Yagi, T.1
  • 35
    • 0030070202 scopus 로고    scopus 로고
    • Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases
    • Satoh, T., Miyoshi, H., Sakamoto, K., and Iwamura, H. (1996) Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases, Biochim. Biophys. Acta 1273, 21-30.
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 21-30
    • Satoh, T.1    Miyoshi, H.2    Sakamoto, K.3    Iwamura, H.4
  • 36
    • 0037995650 scopus 로고    scopus 로고
    • Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone
    • Amarneh, B., and Vik, S. B. (2003) Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone, Biochemistry 42, 4800-4808.
    • (2003) Biochemistry , vol.42 , pp. 4800-4808
    • Amarneh, B.1    Vik, S.B.2
  • 37
    • 0035910270 scopus 로고    scopus 로고
    • Predicting tmasmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., Von Heijne, G., and Sonnhammer, E. L. L. (2001) Predicting tmasmembrane protein topology with a hidden Markov model: application to complete genomes, J. Mol. Biol. 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 38
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and Von Heijne, G. (1994) TopPred II: an improved software for membrane protein structure predictions, Comput. Appl. Biosci. 10, 685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 39
    • 0000207681 scopus 로고
    • tmbase - A database of membrane spanning proteins segments
    • Hofmann, K., and Stoffel, W. (1993) tmbase-a database of membrane spanning proteins segments, Biol. Chem. Hoppe-Seyler 374, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 40
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnády, G. E., and Simon, I. (2001) The HMMTOP transmembrane topology prediction server, Bioinformatics 17, 849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 41
    • 0037077251 scopus 로고    scopus 로고
    • Species-specific and mutant MWFE proteins: Their effect on the assembly of a functional mammalian mitochondrial complex I
    • Yadava, N., Potluri, P., Smith, E. N., Bisevac, A., and Scheffler, I. E. (2002) Species-specific and mutant MWFE proteins: their effect on the assembly of a functional mammalian mitochondrial complex I, J. Biol. Chem. 277, 21221-21230.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21221-21230
    • Yadava, N.1    Potluri, P.2    Smith, E.N.3    Bisevac, A.4    Scheffler, I.E.5
  • 42
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX, Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.