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Volumn 191, Issue 7, 2009, Pages 2091-2101

Differential interactions between tat-specific redox enzyme peptides and their chaperones

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN REDUCTASE; BIOTIN SULFOXIDE REDUCTASE 1; CARRIER PROTEIN; CHAPERONE; DIMETHYL SULFOXIDE REDUCTASE; FORMATE DEHYDROGENASE; HYDROGENASE 1; HYDROGENASE 2; NITRATE REDUCTASE; SIGNAL PEPTIDE; TRIMETHYLAMINE OXIDE REDUCTASE; TWIN ARGININE TRANSLOCASE; UNCLASSIFIED DRUG; ARGININE; ESCHERICHIA COLI PROTEIN; TWIN ARGININE TRANSLOCASE COMPLEX, E COLI; TWIN-ARGININE TRANSLOCASE COMPLEX, E COLI;

EID: 64049092491     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00949-08     Document Type: Article
Times cited : (34)

References (31)
  • 2
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:393-404.
    • (1996) Mol. Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 3
    • 56649102164 scopus 로고    scopus 로고
    • Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone
    • Buchanan, G., J. Maillard, S. B. Nabuurs, D. J. Richardson, T. Palmer, and F. Sargent. 2008. Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone. FEBS Lett. 582:3979- 3984.
    • (2008) FEBS Lett , vol.582 , pp. 3979-3984
    • Buchanan, G.1    Maillard, J.2    Nabuurs, S.B.3    Richardson, D.J.4    Palmer, T.5    Sargent, F.6
  • 4
    • 33645108100 scopus 로고    scopus 로고
    • Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli
    • Chan, C. S., J. M. Howell, M. L. Workentine, and R. J. Turner. 2006. Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. Biochem. Biophys. Res. Commun. 343:244-251.
    • (2006) Biochem. Biophys. Res. Commun , vol.343 , pp. 244-251
    • Chan, C.S.1    Howell, J.M.2    Workentine, M.L.3    Turner, R.J.4
  • 6
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: Identification of precursor-binding accessory proteins
    • Dubini, A., and F. Sargent. 2003. Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett. 549:141-146.
    • (2003) FEBS Lett , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 9
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 11
    • 29144463453 scopus 로고    scopus 로고
    • The role of redox enzyme maturation proteins (REMPs) in the biogenesis of Escherichia coli oxidoreductases: The example of DMSO reductase
    • Howell, J. M., and R. J. Turner. 2004. The role of redox enzyme maturation proteins (REMPs) in the biogenesis of Escherichia coli oxidoreductases: the example of DMSO reductase. Recent Res. Dev. Microbiol. 8:1-14.
    • (2004) Recent Res. Dev. Microbiol , vol.8 , pp. 1-14
    • Howell, J.M.1    Turner, R.J.2
  • 12
    • 1942505361 scopus 로고    scopus 로고
    • Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins
    • Ilbert, M., V. Mejean, and C. Iobbi-Nivol. 2004. Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins. Microbiology 150:935-943.
    • (2004) Microbiology , vol.150 , pp. 935-943
    • Ilbert, M.1    Mejean, V.2    Iobbi-Nivol, C.3
  • 14
    • 0035151432 scopus 로고    scopus 로고
    • Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system
    • Karimova, G., A. Ullmann, and D. Ladant. 2001. Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system. J. Mol. Microbiol. Biotechnol. 3:73-82.
    • (2001) J. Mol. Microbiol. Biotechnol , vol.3 , pp. 73-82
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 15
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., N. Dautin, and D. Ladant. 2005. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187:2233-2243.
    • (2005) J. Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 18
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and J. E. Walker. 1996. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 19
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms
    • Natale, P., T. Brüser, and A. J. M. Driessen. 2008. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms. Biochim. Biophys. Acta 1778:1735-1756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Brüser, T.2    Driessen, A.J.M.3
  • 20
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik, I. J., C. L. Ladner, and R. J. Turner. 2001. Identification of a twin-arginine leader-binding protein. Mol. Microbiol. 40:323-331.
    • (2001) Mol. Microbiol , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 21
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine Noxide reductase enzyme (TorA) in Escherichia coli
    • Pommier, J., V. Mejean, G. Giordano, and C. Iobbi-Nivol. 1998. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine Noxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273: 16615-16620.
    • (1998) J. Biol. Chem , vol.273 , pp. 16615-16620
    • Pommier, J.1    Mejean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 22
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice, P., I. Longden, and A. Bleasby. 2000. EMBOSS: The European Molecular Biology Open Software Suite. Trends Genet. 16:276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 23
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. 2000. Bacterial respiration: a flexible process for a changing environment. Microbiology 146:551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 24
    • 0034698130 scopus 로고    scopus 로고
    • Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli
    • Sambasivarao, D., R. J. Turner, J. L. Simala-Grant, G. Shaw, J. Hu, and J. H. Weiner. 2000. Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 275:22526- 22531.
    • (2000) J. Biol. Chem , vol.275 , pp. 22526-22531
    • Sambasivarao, D.1    Turner, R.J.2    Simala-Grant, J.L.3    Shaw, G.4    Hu, J.5    Weiner, J.H.6
  • 25
    • 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
    • Santini, C.-L., A. Bernadac, M. Zhang, A. Chanal, B. Ize, C. Blanco, and L.-F. Wu. 2001. 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. 276:8159-8164.
    • (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
  • 27
    • 33947370894 scopus 로고    scopus 로고
    • Constructing the wonders of the bacterial world: Biosynthesis of complex enzymes
    • Sargent, F. 2007. Constructing the wonders of the bacterial world: biosynthesis of complex enzymes. Microbiology 153:633-651.
    • (2007) Microbiology , vol.153 , pp. 633-651
    • Sargent, F.1
  • 28
    • 0034307355 scopus 로고    scopus 로고
    • Uses of lacZ to study gene function: Evaluation of -galactosidase assays employed in the yeast twohybrid system
    • Serebriiskii, I. G., and E. A. Golemis. 2000. Uses of lacZ to study gene function: evaluation of -galactosidase assays employed in the yeast twohybrid system. Anal. Biochem. 285:1-15.
    • (2000) Anal. Biochem , vol.285 , pp. 1-15
    • Serebriiskii, I.G.1    Golemis, E.A.2
  • 29
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • Turner, R. J., A. L. Papish, and F. Sargent. 2004. Sequence analysis of bacterial redox enzyme maturation proteins (REMPs). Can. J. Microbiol. 50:225-238.
    • (2004) Can. J. Microbiol , vol.50 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 30
    • 33644872480 scopus 로고    scopus 로고
    • NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly
    • Vergnes, A., J. Pommier, R. Toci, F. Blasco, G. Giordano, and A. Magalon. 2006. NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly. J. Biol. Chem. 281:2170-2176.
    • (2006) J. Biol. Chem , vol.281 , pp. 2170-2176
    • Vergnes, A.1    Pommier, J.2    Toci, R.3    Blasco, F.4    Giordano, G.5    Magalon, A.6


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