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Volumn 583, Issue 17, 2009, Pages 2849-2853

Impairment of twin-arginine-dependent export by seemingly small alterations of substrate conformation

Author keywords

Protein secretion; Quality control; Tat translocase; Twin arginine

Indexed keywords

ALKALINE PHOSPHATASE; CARRIER PROTEIN; CYSTEINE; OXIDOREDUCTASE; PROTEINASE K; TAT TRANSLOCASE; TRIMETHYLAMINE OXIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 69249221229     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.07.038     Document Type: Article
Times cited : (18)

References (15)
  • 1
    • 69249236853 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway
    • Wooldridge K. (Ed), Caister Academic Press, Norfolk, UK
    • Panahandeh S., Holzapfel E., and Müller M. The twin-arginine translocation pathway. In: Wooldridge K. (Ed). Bacterial Secreted Proteins (2009), Caister Academic Press, Norfolk, UK 23-43
    • (2009) Bacterial Secreted Proteins , pp. 23-43
    • Panahandeh, S.1    Holzapfel, E.2    Müller, M.3
  • 2
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M., and Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276 (2001) 20213-20219
    • (2001) J. Biol. Chem. , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
  • 4
    • 36348950408 scopus 로고    scopus 로고
    • Functional Tat transport of unstructured, small, hydrophilic proteins
    • Richter S., Lindenstrauss U., Lucke C., Bayliss R., and Brüser T. Functional Tat transport of unstructured, small, hydrophilic proteins. J. Biol. Chem. 282 (2007) 33257-33264
    • (2007) J. Biol. Chem. , vol.282 , pp. 33257-33264
    • Richter, S.1    Lindenstrauss, U.2    Lucke, C.3    Bayliss, R.4    Brüser, T.5
  • 5
    • 34447307436 scopus 로고    scopus 로고
    • Evidence for a dynamic and transient pathway through the TAT protein transport machinery
    • Cline K., and McCaffery M. Evidence for a dynamic and transient pathway through the TAT protein transport machinery. EMBO J. 26 (2007) 3039-3049
    • (2007) EMBO J. , vol.26 , pp. 3039-3049
    • Cline, K.1    McCaffery, M.2
  • 6
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa M.P., Tullman D., and Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci USA 100 (2003) 6115-6120
    • (2003) Proc. Natl. Acad. Sci USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 7
    • 57749105440 scopus 로고    scopus 로고
    • Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli
    • Panahandeh S., Maurer C., Moser M., DeLisa M.P., and Müller M. Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli. J. Biol. Chem. 283 (2008) 33267-33275
    • (2008) J. Biol. Chem. , vol.283 , pp. 33267-33275
    • Panahandeh, S.1    Maurer, C.2    Moser, M.3    DeLisa, M.P.4    Müller, M.5
  • 8
    • 49149088292 scopus 로고    scopus 로고
    • The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules
    • Matos C.F., Robinson C., and Di Cola A. The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J. 27 (2008) 2055-2063
    • (2008) EMBO J. , vol.27 , pp. 2055-2063
    • Matos, C.F.1    Robinson, C.2    Di Cola, A.3
  • 9
    • 30044442673 scopus 로고    scopus 로고
    • Targeting of unfolded PhoA to the TAT translocon of Escherichia coli
    • Richter S., and Brüser T. Targeting of unfolded PhoA to the TAT translocon of Escherichia coli. J. Biol. Chem. 280 (2005) 42723-42730
    • (2005) J. Biol. Chem. , vol.280 , pp. 42723-42730
    • Richter, S.1    Brüser, T.2
  • 10
    • 0025737880 scopus 로고
    • Use of in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase and for epitope mapping of monoclonal antibodies
    • Lesley S.A., Brow M.A., and Burgess R.R. Use of in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase and for epitope mapping of monoclonal antibodies. J. Biol. Chem. 266 (1991) 2632-2638
    • (1991) J. Biol. Chem. , vol.266 , pp. 2632-2638
    • Lesley, S.A.1    Brow, M.A.2    Burgess, R.R.3
  • 11
    • 36549072024 scopus 로고    scopus 로고
    • In vitro analysis of the bacterial twin-arginine-dependent protein export
    • Moser M., Panahandeh S., Holzapfel E., and Müller M. In vitro analysis of the bacterial twin-arginine-dependent protein export. Methods Mol. Biol. 390 (2007) 63-80
    • (2007) Methods Mol. Biol. , vol.390 , pp. 63-80
    • Moser, M.1    Panahandeh, S.2    Holzapfel, E.3    Müller, M.4
  • 12
    • 0025357506 scopus 로고
    • SecY protein, a membrane-embedded secretion factor of E. Coli, is cleaved by the ompT protease in vitro
    • Akiyama Y., and Ito K. SecY protein, a membrane-embedded secretion factor of E. Coli, is cleaved by the ompT protease in vitro. Biochem. Biophys. Res. Commun. 167 (1990) 711-715
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 711-715
    • Akiyama, Y.1    Ito, K.2
  • 13
    • 0037036383 scopus 로고    scopus 로고
    • Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli
    • Alami M., Trescher D., Wu L.F., and Müller M. Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J. Biol. Chem. 277 (2002) 20499-20503
    • (2002) J. Biol. Chem. , vol.277 , pp. 20499-20503
    • Alami, M.1    Trescher, D.2    Wu, L.F.3    Müller, M.4
  • 14
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr T.L., and Wickner W.T. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20 (2001) 2472-2479
    • (2001) EMBO J. , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2
  • 15
    • 20444390656 scopus 로고    scopus 로고
    • Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase
    • Wang J., Stieglitz K.A., and Kantrowitz E.R. Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. Biochemistry 44 (2005) 8378-8386
    • (2005) Biochemistry , vol.44 , pp. 8378-8386
    • Wang, J.1    Stieglitz, K.A.2    Kantrowitz, E.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.