메뉴 건너뛰기




Volumn 383, Issue 3, 2004, Pages 537-542

Maturation of the unusual single-cysteine (XXXCH) mitochondrial c-type cytochromes found in trypanosomatids must occur through a novel biogenesis pathway

Author keywords

C type cytochrome; Cytochrome c biogenesis; Euglena; Mitochondrial respiratory chain; Oxidative phosphorylation; Trypanosome

Indexed keywords

BINDING ENERGY; ESCHERICHIA COLI; ETHERS; GENES; PLANTS (BOTANY); POLYPEPTIDES; PROTEINS;

EID: 9144261717     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040832     Document Type: Article
Times cited : (57)

References (49)
  • 1
    • 0038072139 scopus 로고    scopus 로고
    • Haem-polypeptide interactions during cytochrome c maturation
    • Thöny-Meyer, L. (2000) Haem-polypeptide interactions during cytochrome c maturation. Biochim. Biophys. Acta 1459, 316-324
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 316-324
    • Thöny-Meyer, L.1
  • 2
    • 0033573140 scopus 로고    scopus 로고
    • Still a puzzle: Why is haem covalently attached in c-type cytochromes?
    • Barker, P. D. and Ferguson, S. J. (1999) Still a puzzle: why is haem covalently attached in c-type cytochromes? Struct. Fold Des. 7, R281-R290
    • (1999) Struct. Fold Des. , vol.7
    • Barker, P.D.1    Ferguson, S.J.2
  • 3
    • 0242552244 scopus 로고    scopus 로고
    • Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system
    • Allen, J. W. A. and Ferguson, S. J. (2003) Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system. Biochem. J. 375, 721-728
    • (2003) Biochem. J. , vol.375 , pp. 721-728
    • Allen, J.W.A.1    Ferguson, S.J.2
  • 8
    • 0346101796 scopus 로고    scopus 로고
    • 562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system
    • 562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system. J. Biol. Chem. 278, 52075-52083
    • (2003) J. Biol. Chem. , vol.278 , pp. 52075-52083
    • Allen, J.W.A.1    Barker, P.D.2    Ferguson, S.J.3
  • 9
    • 0016698780 scopus 로고
    • Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti
    • Pettigrew, G. W., Leaver, J. L., Meyer, T. E. and Ryle, A. P. (1975) Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti. Biochem. J. 147, 291-302
    • (1975) Biochem. J. , vol.147 , pp. 291-302
    • Pettigrew, G.W.1    Leaver, J.L.2    Meyer, T.E.3    Ryle, A.P.4
  • 11
    • 0025730678 scopus 로고
    • Amino acid sequences of Euglena viridis ferredoxin and cytochromes c
    • Ambler, R. P., Kamen, M. D., Bartsch, R. G. and Meyer, T. E. (1991) Amino acid sequences of Euglena viridis ferredoxin and cytochromes c. Biochem. J. 276, 47-52
    • (1991) Biochem. J. , vol.276 , pp. 47-52
    • Ambler, R.P.1    Kamen, M.D.2    Bartsch, R.G.3    Meyer, T.E.4
  • 13
    • 0023796283 scopus 로고
    • Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei
    • Torri, A. F. and Hajduk, S. L. (1988) Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei. Mol. Cell. Biol. 8, 4625-4633
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4625-4633
    • Torri, A.F.1    Hajduk, S.L.2
  • 14
    • 0038771140 scopus 로고    scopus 로고
    • Cytochrome f and subunit IV, two essential components of the photosynthetic of complex typically encoded in the chloroplast genome, are nucleus-encoded in Euglena gracilis
    • Santillan Torres, J. L., Atteia, A., Claros, M. G. and Gonzalez-Halphen, D. (2003) Cytochrome f and subunit IV, two essential components of the photosynthetic of complex typically encoded in the chloroplast genome, are nucleus-encoded in Euglena gracilis. Biochim. Biophys. Acta 1604, 180-189
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 180-189
    • Santillan Torres, J.L.1    Atteia, A.2    Claros, M.G.3    Gonzalez-Halphen, D.4
  • 15
    • 0016249793 scopus 로고
    • The purification and amino acid sequence of cytochrome C-552 from Euglena gracilis
    • Pettigrew, G. W. (1974) The purification and amino acid sequence of cytochrome C-552 from Euglena gracilis. Biochem. J. 139, 449-459
    • (1974) Biochem. J. , vol.139 , pp. 449-459
    • Pettigrew, G.W.1
  • 16
    • 0036156055 scopus 로고    scopus 로고
    • Genomic analyses of bacterial respiratory and cytochrome c assembly systems: Bordetella as a model for the system II cytochrome c biogenesis pathway
    • Kranz, R. G., Beckett, C. S. and Goldman, B. S. (2002) Genomic analyses of bacterial respiratory and cytochrome c assembly systems: Bordetella as a model for the system II cytochrome c biogenesis pathway. Res. Microbiol. 153, 1-6
    • (2002) Res. Microbiol. , vol.153 , pp. 1-6
    • Kranz, R.G.1    Beckett, C.S.2    Goldman, B.S.3
  • 17
    • 0033868211 scopus 로고    scopus 로고
    • Assembly of chloroplast cytochromes b and c
    • Nakamoto, S. S., Hamel, P. and Merchant, S. (2000) Assembly of chloroplast cytochromes b and c. Biochimie 82, 603-614
    • (2000) Biochimie , vol.82 , pp. 603-614
    • Nakamoto, S.S.1    Hamel, P.2    Merchant, S.3
  • 18
    • 0028290650 scopus 로고
    • A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria
    • Hussain, H., Grove, J., Griffiths, L, Busby, S. and Cole, J. (1994) A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. Mol. Microbiol. 12, 153-163
    • (1994) Mol. Microbiol. , vol.12 , pp. 153-163
    • Hussain, H.1    Grove, J.2    Griffiths, L.3    Busby, S.4    Cole, J.5
  • 20
    • 0037072786 scopus 로고    scopus 로고
    • The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c
    • Allen, J. W. A., Tomlinson, E. J., Hong, L. and Ferguson, S. J. (2002) The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c. J. Biol. Chem. 277, 33559-33563
    • (2002) J. Biol. Chem. , vol.277 , pp. 33559-33563
    • Allen, J.W.A.1    Tomlinson, E.J.2    Hong, L.3    Ferguson, S.J.4
  • 21
    • 33750622183 scopus 로고
    • Cytochromes: Bacterial
    • Bartsch, R. G. (1971) Cytochromes: bacterial. Methods Enzymol. 23, 344-363
    • (1971) Methods Enzymol. , vol.23 , pp. 344-363
    • Bartsch, R.G.1
  • 22
    • 0034058146 scopus 로고    scopus 로고
    • Genes required for cytochrome c synthesis in Bacillus subtilis
    • Le Brun, N. E., Bengtsson, J. and Hederstedt, L. (2000) Genes required for cytochrome c synthesis in Bacillus subtilis. Mol. Microbiol. 36, 638-650
    • (2000) Mol. Microbiol. , vol.36 , pp. 638-650
    • Le Brun, N.E.1    Bengtsson, J.2    Hederstedt, L.3
  • 23
    • 0037462683 scopus 로고    scopus 로고
    • Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis
    • Dreyfuss, B. W., Hamel, P. P., Nakamoto, S. S. and Merchant, S. (2003) Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis. J. Biol. Chem. 278, 2604-2613
    • (2003) J. Biol. Chem. , vol.278 , pp. 2604-2613
    • Dreyfuss, B.W.1    Hamel, P.P.2    Nakamoto, S.S.3    Merchant, S.4
  • 24
    • 0037462720 scopus 로고    scopus 로고
    • Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein
    • Hamel, P. P., Dreyfuss, B. W., Xie, Z., Gabilly, S. T. and Merchant, S. (2003) Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein. J. Biol. Chem. 278, 2593-2603
    • (2003) J. Biol. Chem. , vol.278 , pp. 2593-2603
    • Hamel, P.P.1    Dreyfuss, B.W.2    Xie, Z.3    Gabilly, S.T.4    Merchant, S.5
  • 26
    • 0038351001 scopus 로고    scopus 로고
    • 1 is imported into mitochondria along an unusual pathway
    • 1 is imported into mitochondria along an unusual pathway. J. Biol. Chem. 278, 15084-15094
    • (2003) J. Biol. Chem. , vol.278 , pp. 15084-15094
    • Priest, J.W.1    Hajduk, S.L.2
  • 28
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira, A. and Duarte, M. (2002) From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta 1555, 187-191
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 29
    • 0040187760 scopus 로고    scopus 로고
    • Detection of the mitochondrially encoded cytochrome c oxidase subunit I in the trypanosomatid protozoan Leishmania tarentolae. Evidence for translation of unedited mRNA in the kinetoplast
    • Horvath, A., Kingan, T. G. and Maslov, D. A. (2000) Detection of the mitochondrially encoded cytochrome c oxidase subunit I in the trypanosomatid protozoan Leishmania tarentolae. Evidence for translation of unedited mRNA in the kinetoplast. J. Biol. Chem. 275, 17160-17165
    • (2000) J. Biol. Chem. , vol.275 , pp. 17160-17165
    • Horvath, A.1    Kingan, T.G.2    Maslov, D.A.3
  • 30
    • 0029278815 scopus 로고
    • Molecular features and mitochondrial import pathway of the 14-kilodalton subunit of cytochrome c reductase from potato
    • Braun, H. P. and Schmilz, U. K. (1995) Molecular features and mitochondrial import pathway of the 14-kilodalton subunit of cytochrome c reductase from potato. Plant Physiol. 107, 1217-1223
    • (1995) Plant Physiol. , vol.107 , pp. 1217-1223
    • Braun, H.P.1    Schmilz, U.K.2
  • 31
    • 0028290026 scopus 로고
    • The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence
    • Braun, H. P., Jansch, L., Kurft, V. and Schmilz, U. K. (1994) The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence. FEBS Lett. 347, 90-94
    • (1994) FEBS Lett. , vol.347 , pp. 90-94
    • Braun, H.P.1    Jansch, L.2    Kurft, V.3    Schmilz, U.K.4
  • 36
    • 0032524917 scopus 로고    scopus 로고
    • 552 gene from Thermus thermophilus HB8. Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products
    • 552 gene from Thermus thermophilus HB8. Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products. J. Biol. Chem. 273, 12006-12016
    • (1998) J. Biol. Chem. , vol.273 , pp. 12006-12016
    • Keightley, J.A.1    Sanders, D.2    Todaro, T.R.3    Pastuszyn, A.4    Fee, J.A.5
  • 39
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock, W. B., Rosell, F. I., Twitchett, M. B., Dumont, M. E. and Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37, 6124-6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 41
    • 0037184910 scopus 로고    scopus 로고
    • Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis
    • Martin, A. G. and Fearnhead, H. O. (2002) Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis. J. Biol. Chem. 277, 50834-50841
    • (2002) J. Biol. Chem. , vol.277 , pp. 50834-50841
    • Martin, A.G.1    Fearnhead, H.O.2
  • 42
    • 0037129949 scopus 로고    scopus 로고
    • Spectroscopic properties of a mitochondrial cytochrome c with a single thioether bond to the heme prosthetic group
    • Rosell, F. I. and Mauk, A. G. (2002) Spectroscopic properties of a mitochondrial cytochrome c with a single thioether bond to the heme prosthetic group. Biochemistry 41, 7811-7818
    • (2002) Biochemistry , vol.41 , pp. 7811-7818
    • Rosell, F.I.1    Mauk, A.G.2
  • 43
    • 0034693154 scopus 로고    scopus 로고
    • Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties
    • Tomlinson, E. J. and Ferguson, S. J. (2000) Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties. J. Biol. Chem. 275, 32530-32534
    • (2000) J. Biol. Chem. , vol.275 , pp. 32530-32534
    • Tomlinson, E.J.1    Ferguson, S.J.2
  • 49
    • 2542448350 scopus 로고    scopus 로고
    • Did trypanosomatid parasites have photosynthetic ancestors?
    • Leander, B. S. (2004) Did trypanosomatid parasites have photosynthetic ancestors? Trends Microbiol. 12, 251-258
    • (2004) Trends Microbiol. , vol.12 , pp. 251-258
    • Leander, B.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.