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Volumn 85, Issue 6, 2003, Pages 575-579

Effect of alteration of the C-terminal extension on the maturation and folding of the large subunit of the Escherichia coli hydrogenase-2

Author keywords

Folding; GFP; Hydrogenase; Maturation; Nickel

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYDROGENASE; HYDROGENASE 2; IRON; NICKEL; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 0038760111     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(03)00091-9     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • L.-F. Wu, M.A. Mandrand, Microbial hydrogenases: Primary structure, classification, signatures and phylogeny, FEMS Microbiol. Rev. 10 (1993) 243-269.
    • (1993) FEMS Microbiol. Rev. , vol.10 , pp. 243-269
    • Wu, L.-F.1    Mandrand, M.A.2
  • 3
    • 0035340936 scopus 로고    scopus 로고
    • Maturation of the [NiFe] hydrogenases
    • L. Casalot, M. Rousset, Maturation of the [NiFe] hydrogenases, Trends Microbiol. 9 (2001) 228-237.
    • (2001) Trends Microbiol. , vol.9 , pp. 228-237
    • Casalot, L.1    Rousset, M.2
  • 5
    • 0026714545 scopus 로고
    • Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii
    • D.J. Gollin, L.E. Mortenson, R.L. Robson, Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii, FEBS Lett. 309 (1992) 371-375.
    • (1992) FEBS Lett. , vol.309 , pp. 371-375
    • Gollin, D.J.1    Mortenson, L.E.2    Robson, R.L.3
  • 6
    • 0027233609 scopus 로고
    • A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is posttranslationally processed by cleavage at a defined position
    • O. Sorgenfrei, D. Linder, M. Karas, A. Klein, A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is posttranslationally processed by cleavage at a defined position, Eur. J. Biochem. 213 (1993) 1355-1358.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1355-1358
    • Sorgenfrei, O.1    Linder, D.2    Karas, M.3    Klein, A.4
  • 8
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • R. Rossmann, M. Sauter, F. Lottspeich, A. Böck, Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537, Eur. J. Biochem. 220 (1994) 377-384.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Böck, A.4
  • 9
    • 0030012735 scopus 로고    scopus 로고
    • Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product
    • S. Thiemermann, J. Dernedde, M. Bernhard, W. Schroeder, C. Massanz, B. Friedrich, Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product, J. Bacteriol. 178 (1996) 2368-2374.
    • (1996) J. Bacteriol. , vol.178 , pp. 2368-2374
    • Thiemermann, S.1    Dernedde, J.2    Bernhard, M.3    Schroeder, W.4    Massanz, C.5    Friedrich, B.6
  • 10
    • 0033591263 scopus 로고    scopus 로고
    • Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli
    • E. Fritsche, A. Paschos, H.G. Beisel, A. Böck, R. Huber, Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli, J. Mol. Biol. 288 (1999) 989-998.
    • (1999) J. Mol. Biol. , vol.288 , pp. 989-998
    • Fritsche, E.1    Paschos, A.2    Beisel, H.G.3    Böck, A.4    Huber, R.5
  • 11
    • 0001789455 scopus 로고    scopus 로고
    • Nickel incorporation into hydrogenases
    • in: R.P. Hausinger, G.L. Eichhorn, L.G. Marzilli (Eds.); VCH Publishers, Inc., New York
    • T. Maier, A. Böck, Nickel incorporation into hydrogenases, in: R.P. Hausinger, G.L. Eichhorn, L.G. Marzilli (Eds.), Mechanisms of Metallocenter Assembly, VCH Publishers, Inc., New York, 1996, pp. 173-192.
    • (1996) Mechanisms of Metallocenter Assembly , pp. 173-192
    • Maier, T.1    Böck, A.2
  • 12
    • 0033961397 scopus 로고    scopus 로고
    • Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli
    • E. Theodoratou, A. Paschos, S. Mintz-Weber, A. Böck, Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli, Arch. Microbiol. 173 (2000) 110-116.
    • (2000) Arch. Microbiol. , vol.173 , pp. 110-116
    • Theodoratou, E.1    Paschos, A.2    Mintz-Weber, S.3    Böck, A.4
  • 15
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu
    • M.J. Casadaban, Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu, J. Mol. Biol. 104 (1976) 541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 16
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • M. Chalfie, Y. Tu, G. Euskirchen, W.W. Ward, D.C. Prasher, Green fluorescent protein as a marker for gene expression, Science 263 (1994) 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • J.H. Miller, Experiments in Molecular Genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1972.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 18
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • C.-L. Santini, A. Bernadac, M. Zhang, A. Chanal, B. Ize, C. Blanco, L.-F. Wu, Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock, J. Biol. Chem. 276 (2001) 8159-8164.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8159-8164
    • Santini, C.-L.1    Bernadac, A.2    Zhang, M.3    Chanal, A.4    Ize, B.5    Blanco, C.6    Wu, L.-F.7
  • 19
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • S.P. Ballantine, D.H. Boxer, Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12, J. Bacteriol. 163 (1985) 454-459.
    • (1985) J. Bacteriol. , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 20
    • 0030603123 scopus 로고    scopus 로고
    • Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli
    • A. Rodrigue, D.H. Boxer, M.A. Mandrand-Berthelot, L.-F. Wu, Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli, FEBS Lett. 392 (1996) 81-86.
    • (1996) FEBS Lett. , vol.392 , pp. 81-86
    • Rodrigue, A.1    Boxer, D.H.2    Mandrand-Berthelot, M.A.3    Wu, L.-F.4
  • 21
    • 0024836127 scopus 로고
    • Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli
    • L.-F. Wu, M.A. Mandrand-Berthelot, R. Waugh, C.J. Edmonds, S.E. Holt, D.H. Boxer, Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli, Mol. Microbiol. 3 (1989) 1709-1718.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1709-1718
    • Wu, L.-F.1    Mandrand-Berthelot, M.A.2    Waugh, R.3    Edmonds, C.J.4    Holt, S.E.5    Boxer, D.H.6
  • 22
    • 0027482679 scopus 로고
    • The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel
    • C. Navarro, L.-F. Wu, M.A. Mandrand-Berthelot, The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel, Mol. Microbiol. 9 (1993) 1181-1191.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1181-1191
    • Navarro, C.1    Wu, L.-F.2    Mandrand-Berthelot, M.A.3
  • 23
    • 0029745210 scopus 로고    scopus 로고
    • Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli
    • A. Rodrigue, N. Batia, M. Müller, O. Fayet, R. Böhm, M.A. Mandrand-Berthelot, L.-F. Wu, Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli, J. Bacteriol. 178 (1996) 4453-4460.
    • (1996) J. Bacteriol. , vol.178 , pp. 4453-4460
    • Rodrigue, A.1    Batia, N.2    Müller, M.3    Fayet, O.4    Böhm, R.5    Mandrand-Berthelot, M.A.6    Wu, L.-F.7
  • 24
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • D.E. Drew, G. Von Heijne, P. Nordlund, J.W. De Gier, Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli, FEBS Lett. 507 (2001) 220-224.
    • (2001) FEBS Lett. , vol.507 , pp. 220-224
    • Drew, D.E.1    Von Heijne, G.2    Nordlund, P.3    De Gier, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.