메뉴 건너뛰기




Volumn 53, Issue 32, 2014, Pages 5261-5271

Conserved residues of the human mitochondrial holocytochrome c synthase mediate interactions with heme

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; ENZYME ACTIVITY;

EID: 84906275081     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500704p     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c Cell 86, 147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 56349110794 scopus 로고    scopus 로고
    • Biochemical requirements for the maturation of mitochondrial c-type cytochromes
    • Hamel, P., Corvest, V., Giege, P., and Bonnard, G. (2009) Biochemical requirements for the maturation of mitochondrial c-type cytochromes Biochim. Biophys. Acta 1793, 125-138
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 125-138
    • Hamel, P.1    Corvest, V.2    Giege, P.3    Bonnard, G.4
  • 4
    • 80255134546 scopus 로고    scopus 로고
    • Cytochrome c biogenesis in mitochondria - Systems III and v
    • Allen, J. W. (2011) Cytochrome c biogenesis in mitochondria - Systems III and V FEBS J. 278, 4198-4216
    • (2011) FEBS J. , vol.278 , pp. 4198-4216
    • Allen, J.W.1
  • 6
    • 0024408905 scopus 로고
    • Import of cytochrome c into mitochondria: Reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c
    • Nicholson, D. W. and Neupert, W. (1989) Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c Proc. Natl. Acad. Sci. U. S. A. 86, 4340-4344
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 4340-4344
    • Nicholson, D.W.1    Neupert, W.2
  • 7
    • 0023067403 scopus 로고
    • Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae
    • Dumont, M. E., Ernst, J. F., Hampsey, D. M., and Sherman, F. (1987) Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae EMBO J. 6, 235-241
    • (1987) EMBO J. , vol.6 , pp. 235-241
    • Dumont, M.E.1    Ernst, J.F.2    Hampsey, D.M.3    Sherman, F.4
  • 8
    • 0021879660 scopus 로고
    • On the specificity of cytochrome c synthetase in recognition of the amino acid sequence of apocytochrome c
    • Visco, C., Taniuchi, H., and Berlett, B. S. (1985) On the specificity of cytochrome c synthetase in recognition of the amino acid sequence of apocytochrome c J. Biol. Chem. 260, 6133-6138
    • (1985) J. Biol. Chem. , vol.260 , pp. 6133-6138
    • Visco, C.1    Taniuchi, H.2    Berlett, B.S.3
  • 9
    • 0026681741 scopus 로고
    • Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome-c1-heme lyase
    • Zollner, A., Rodel, G., and Haid, A. (1992) Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome-c1-heme lyase Eur. J. Biochem. 207, 1093-1100
    • (1992) Eur. J. Biochem. , vol.207 , pp. 1093-1100
    • Zollner, A.1    Rodel, G.2    Haid, A.3
  • 10
    • 0346118951 scopus 로고    scopus 로고
    • Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases
    • Bernard, D. G., Gabilly, S. T., Dujardin, G., Merchant, S., and Hamel, P. P. (2003) Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases J. Biol. Chem. 278, 49732-49742
    • (2003) J. Biol. Chem. , vol.278 , pp. 49732-49742
    • Bernard, D.G.1    Gabilly, S.T.2    Dujardin, G.3    Merchant, S.4    Hamel, P.P.5
  • 11
    • 0036900297 scopus 로고    scopus 로고
    • Loss of holocytochrome c-type synthetase causes the male lethality of X-linked dominant microphthalmia with linear skin defects (MLS) syndrome
    • Prakash, S. K., Cormier, T. A., McCall, A. E., Garcia, J. J., Sierra, R., Haupt, B., Zoghbi, H. Y., and Van Den Veyver, I. B. (2002) Loss of holocytochrome c-type synthetase causes the male lethality of X-linked dominant microphthalmia with linear skin defects (MLS) syndrome Hum. Mol. Genet. 11, 3237-3248
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3237-3248
    • Prakash, S.K.1    Cormier, T.A.2    McCall, A.E.3    Garcia, J.J.4    Sierra, R.5    Haupt, B.6    Zoghbi, H.Y.7    Van Den Veyver, I.B.8
  • 12
    • 0029882297 scopus 로고    scopus 로고
    • Cloning and characterization of a putative human holocytochrome c-type synthetase gene (HCCS) isolated from the critical region for microphthalmia with linear skin defects (MLS)
    • Schaefer, L., Ballabio, A., and Zoghbi, H. Y. (1996) Cloning and characterization of a putative human holocytochrome c-type synthetase gene (HCCS) isolated from the critical region for microphthalmia with linear skin defects (MLS) Genomics 34, 166-172
    • (1996) Genomics , vol.34 , pp. 166-172
    • Schaefer, L.1    Ballabio, A.2    Zoghbi, H.Y.3
  • 13
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • Kranz, R. G., Richard-Fogal, C., Taylor, J. S., and Frawley, E. R. (2009) Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control Microbiol. Mol. Biol. Rev. 73, 510-528
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.S.3    Frawley, E.R.4
  • 16
    • 0031688431 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a Candida albicans gene coding for cytochrome c haem lyase and a cell wall-related protein
    • Cervera, A. M., Gozalbo, D., McCreath, K. J., Gow, N. A., Martinez, J. P., and Casanova, M. (1998) Molecular cloning and characterization of a Candida albicans gene coding for cytochrome c haem lyase and a cell wall-related protein Mol. Microbiol. 30, 67-81
    • (1998) Mol. Microbiol. , vol.30 , pp. 67-81
    • Cervera, A.M.1    Gozalbo, D.2    McCreath, K.J.3    Gow, N.A.4    Martinez, J.P.5    Casanova, M.6
  • 17
    • 0024279426 scopus 로고
    • Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c
    • Dumont, M. E., Ernst, J. F., and Sherman, F. (1988) Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c J. Biol. Chem. 263, 15928-15937
    • (1988) J. Biol. Chem. , vol.263 , pp. 15928-15937
    • Dumont, M.E.1    Ernst, J.F.2    Sherman, F.3
  • 18
    • 0025989267 scopus 로고
    • Role of cytochrome c heme lyase in mitochondrial import and accumulation of cytochrome c in Saccharomyces cerevisiae
    • Dumont, M. E., Cardillo, T. S., Hayes, M. K., and Sherman, F. (1991) Role of cytochrome c heme lyase in mitochondrial import and accumulation of cytochrome c in Saccharomyces cerevisiae Mol. Cell. Biol. 11, 5487-5496
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5487-5496
    • Dumont, M.E.1    Cardillo, T.S.2    Hayes, M.K.3    Sherman, F.4
  • 19
    • 0024244832 scopus 로고
    • Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria
    • Nicholson, D. W., Hergersberg, C., and Neupert, W. (1988) Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria J. Biol. Chem. 263, 19034-19042
    • (1988) J. Biol. Chem. , vol.263 , pp. 19034-19042
    • Nicholson, D.W.1    Hergersberg, C.2    Neupert, W.3
  • 20
    • 84874480835 scopus 로고    scopus 로고
    • Human mitochondrial holocytochrome c synthases heme binding, maturation determinants, and complex formation with cytochrome c
    • San Francisco, B., Bretsnyder, E. C., and Kranz, R. G. (2013) Human mitochondrial holocytochrome c synthases heme binding, maturation determinants, and complex formation with cytochrome c Proc. Natl. Acad. Sci. U. S. A. 110, E788-797
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 788-797
    • San Francisco, B.1    Bretsnyder, E.C.2    Kranz, R.G.3
  • 21
    • 0032717261 scopus 로고    scopus 로고
    • An internal targeting signal directing proteins into the mitochondrial intermembrane space
    • Diekert, K., Kispal, G., Guiard, B., and Lill, R. (1999) An internal targeting signal directing proteins into the mitochondrial intermembrane space Proc. Natl. Acad. Sci. U. S. A. 96, 11752-11757
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11752-11757
    • Diekert, K.1    Kispal, G.2    Guiard, B.3    Lill, R.4
  • 22
    • 33645809956 scopus 로고    scopus 로고
    • Recombinant cytochromes c biogenesis systems i and II and analysis of haem delivery pathways in Escherichia coli
    • Feissner, R. E., Richard-Fogal, C. L., Frawley, E. R., Loughman, J. A., Earley, K. W., and Kranz, R. G. (2006) Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli Mol. Microbiol. 60, 563-577
    • (2006) Mol. Microbiol. , vol.60 , pp. 563-577
    • Feissner, R.E.1    Richard-Fogal, C.L.2    Frawley, E.R.3    Loughman, J.A.4    Earley, K.W.5    Kranz, R.G.6
  • 23
    • 0037380881 scopus 로고    scopus 로고
    • Chemiluminescent-based methods to detect subpicomole levels of c-type cytochromes
    • Feissner, R., Xiang, Y., and Kranz, R. G. (2003) Chemiluminescent-based methods to detect subpicomole levels of c-type cytochromes Anal. Biochem. 315, 90-94
    • (2003) Anal. Biochem. , vol.315 , pp. 90-94
    • Feissner, R.1    Xiang, Y.2    Kranz, R.G.3
  • 24
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 25
    • 67649878164 scopus 로고    scopus 로고
    • CcsBA is a cytochrome c synthetase that also functions in heme transport
    • Frawley, E. R. and Kranz, R. G. (2009) CcsBA is a cytochrome c synthetase that also functions in heme transport Proc. Natl. Acad. Sci. U. S. A. 106, 10201-10206
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10201-10206
    • Frawley, E.R.1    Kranz, R.G.2
  • 26
    • 34548359346 scopus 로고    scopus 로고
    • HCCS loss-of-function missense mutation in a female with bilateral microphthalmia and sclerocornea: A novel gene for severe ocular malformations?
    • Wimplinger, I., Shaw, G. M., and Kutsche, K. (2007) HCCS loss-of-function missense mutation in a female with bilateral microphthalmia and sclerocornea: a novel gene for severe ocular malformations? Mol. Vis. 13, 1475-1482
    • (2007) Mol. Vis. , vol.13 , pp. 1475-1482
    • Wimplinger, I.1    Shaw, G.M.2    Kutsche, K.3
  • 27
    • 80255137459 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c synthase: CP motifs are not necessary for heme attachment to apocytochrome c
    • Moore, R. L., Stevens, J. M., and Ferguson, S. J. (2011) Mitochondrial cytochrome c synthase: CP motifs are not necessary for heme attachment to apocytochrome c FEBS Lett. 585, 3415-3419
    • (2011) FEBS Lett. , vol.585 , pp. 3415-3419
    • Moore, R.L.1    Stevens, J.M.2    Ferguson, S.J.3
  • 29
    • 0028339218 scopus 로고
    • Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93→ Gly
    • Barrick, D. (1994) Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93→ Gly Biochemistry 33, 6546-6554
    • (1994) Biochemistry , vol.33 , pp. 6546-6554
    • Barrick, D.1
  • 30
    • 83455221648 scopus 로고    scopus 로고
    • Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF
    • San Francisco, B., Bretsnyder, E. C., Rodgers, K. R., and Kranz, R. G. (2011) Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF Biochemistry 50, 10974-10985
    • (2011) Biochemistry , vol.50 , pp. 10974-10985
    • San Francisco, B.1    Bretsnyder, E.C.2    Rodgers, K.R.3    Kranz, R.G.4
  • 32
    • 0028984985 scopus 로고
    • Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli
    • Kery, V., Elleder, D., and Kraus, J. P. (1995) Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli Arch. Biochem. Biophys. 316, 24-29
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 24-29
    • Kery, V.1    Elleder, D.2    Kraus, J.P.3
  • 33
    • 79952107782 scopus 로고    scopus 로고
    • Structural analysis of heme proteins: Implications for design and prediction
    • Li, T., Bonkovsky, H. L., and Guo, J. T. (2011) Structural analysis of heme proteins: implications for design and prediction BMC Struct. Biol. 11, 13
    • (2011) BMC Struct. Biol. , vol.11 , pp. 13
    • Li, T.1    Bonkovsky, H.L.2    Guo, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.