메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Signal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SECA; RECEPTOR PROTEIN; SECRETORY PROTEIN; SIGNAL RECOGNITION PARTICLE; TRANSLOCON; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARRIER PROTEIN; CROSS LINKING REAGENT; ESCHERICHIA COLI PROTEIN; SECA PROTEIN, BACTERIA; SIGNAL PEPTIDE;

EID: 84899537656     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0092994     Document Type: Article
Times cited : (10)

References (31)
  • 1
    • 84879888089 scopus 로고    scopus 로고
    • Protein translocation across the inner membrane of Gram-negative bacteria: The Sec and Tat dependent protein transport pathways
    • Kudva R, Denks K, Kuhn P, Vogt A, Müller M, et al. (2013) Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways. Res Microbiol 164: 505-534.
    • (2013) Res Microbiol , vol.164 , pp. 505-534
    • Kudva, R.1    Denks, K.2    Kuhn, P.3    Vogt, A.4    Müller, M.5
  • 2
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang X, Rashid R, Wang K, Shan SO (2010) Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 328: 757-760.
    • (2010) Science , vol.328 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.O.4
  • 3
    • 79951826865 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle in complex with its receptor
    • Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, et al. (2011) The crystal structure of the signal recognition particle in complex with its receptor. Science 331: 881-886.
    • (2011) Science , vol.331 , pp. 881-886
    • Ataide, S.F.1    Schmitz, N.2    Shen, K.3    Ke, A.4    Shan, S.O.5
  • 4
    • 79959912257 scopus 로고    scopus 로고
    • Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle
    • Braig D, Mircheva M, Sachelaru I, van der Sluis EO, Sturm L, et al. (2011) Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle. Mol Biol Cell 22: 2309-2323.
    • (2011) Mol Biol Cell , vol.22 , pp. 2309-2323
    • Braig, D.1    Mircheva, M.2    Sachelaru, I.3    Van Der Sluis, E.O.4    Sturm, L.5
  • 5
    • 84855572511 scopus 로고    scopus 로고
    • Is there a twist in the Escherichia coli signal recognition particle pathway?
    • Bibi E (2012) Is there a twist in the Escherichia coli signal recognition particle pathway? Trends Biochem Sci 37: 1-6.
    • (2012) Trends Biochem Sci , vol.37 , pp. 1-6
    • Bibi, E.1
  • 6
    • 0033605757 scopus 로고    scopus 로고
    • SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle
    • Qi HY, Bernstein HD (1999) SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle. J Biol Chem 274: 8993-8997.
    • (1999) J Biol Chem , vol.274 , pp. 8993-8997
    • Qi, H.Y.1    Bernstein, H.D.2
  • 7
    • 0034712727 scopus 로고    scopus 로고
    • A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
    • DOI 10.1073/pnas.090087297
    • Tian H, Boyd D, Beckwith J (2000) A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. Proc Natl Acad Sci U S A 97: 4730-4735. (Pubitemid 30238626)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.9 , pp. 4730-4735
    • Tian, H.1    Boyd, D.2    Beckwith, J.3
  • 8
    • 0034387983 scopus 로고    scopus 로고
    • SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein
    • Neumann-Haefelin C, Schäfer U, Müller M, Koch HG (2000) SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein. EMBO J 19: 6419-6426.
    • (2000) EMBO J , vol.19 , pp. 6419-6426
    • Neumann-Haefelin, C.1    Schäfer, U.2    Müller, M.3    Koch, H.G.4
  • 9
    • 0347087516 scopus 로고    scopus 로고
    • SecYEG Proteoliposomes Catalyze the Deltapsi-Dependent Membrane Insertion of FtsQ
    • DOI 10.1074/jbc.M306527200
    • van der Laan M, Nouwen N, Driessen AJ (2004) SecYEG proteoliposomes catalyze the Deltapsi-dependent membrane insertion of FtsQ. J Biol Chem 279: 1659-1664. (Pubitemid 38084432)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1659-1664
    • Van Der, L.M.1    Nouwen, N.2    Driessen, A.J.M.3
  • 10
    • 28244452583 scopus 로고    scopus 로고
    • A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli
    • DOI 10.1074/jbc.M509647200
    • Deitermann S, Sprie GS, Koch HG (2005) A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli. J Biol Chem 280: 39077-39085. (Pubitemid 41713858)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39077-39085
    • Deitermann, S.1    Sprie, G.S.2    Koch, H.-G.3
  • 11
    • 0033569759 scopus 로고    scopus 로고
    • SecA is not required for signal recognition particle-mediated targeting and initial membrane insertion of a nascent inner membrane protein
    • Scotti PA, Valent QA, Manting EH, Urbanus ML, Driessen AJ, et al. (1999) SecA is not required for signal recognition particle-mediated targeting and initial membrane insertion of a nascent inner membrane protein. J Biol Chem 274: 29883-29888.
    • (1999) J Biol Chem , vol.274 , pp. 29883-29888
    • Scotti, P.A.1    Valent, Q.A.2    Manting, E.H.3    Urbanus, M.L.4    Driessen, A.J.5
  • 12
    • 43949125856 scopus 로고    scopus 로고
    • The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon
    • DOI 10.1021/bi800233w
    • Antonoaea R, Fürst M, Nishiyama K, Müller M (2008) The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. Biochemistry 47: 5649-5656. (Pubitemid 351705176)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5649-5656
    • Antonoaea, R.1    Furst, M.2    Nishiyama, K.-I.3    Muller, M.4
  • 13
    • 84863407242 scopus 로고    scopus 로고
    • Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle
    • Welte T, Kudva R, Kuhn P, Sturm L, Braig D, et al. (2012) Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle. Mol Biol Cell 23: 464-479.
    • (2012) Mol Biol Cell , vol.23 , pp. 464-479
    • Welte, T.1    Kudva, R.2    Kuhn, P.3    Sturm, L.4    Braig, D.5
  • 14
    • 17644386832 scopus 로고    scopus 로고
    • Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation
    • Huber D, Boyd D, Xia Y, Olma MH, Gerstein M, et al. (2005) Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J Bacteriol 187: 2983-2891.
    • (2005) J Bacteriol , vol.187 , pp. 2983-12891
    • Huber, D.1    Boyd, D.2    Xia, Y.3    Olma, M.H.4    Gerstein, M.5
  • 15
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • DOI 10.1128/JB.185.19.5706-5713.2003
    • Schierle CF, Berkmen M, Huber D, Kumamoto C, Boyd D, et al. (2003) The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J Bacteriol 185: 5706-5713. (Pubitemid 37176482)
    • (2003) Journal of Bacteriology , vol.185 , Issue.19 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 16
    • 20444477153 scopus 로고    scopus 로고
    • Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane
    • DOI 10.1128/JB.187.12.3997-4004.2005
    • Shimohata N, Akiyama Y, Ito K (2005) Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane. J Bacteriol 187: 3997-4004. (Pubitemid 40827783)
    • (2005) Journal of Bacteriology , vol.187 , Issue.12 , pp. 3997-4004
    • Shimohata, N.1    Akiyama, Y.2    Ito, K.3
  • 18
    • 67049100580 scopus 로고    scopus 로고
    • Twin-arginine-dependent translocation of SufI in the absence of cytosolic helper proteins
    • Holzapfel E, Moser M, Schiltz E, Ueda T, Betton JM, et al. (2009) Twin-arginine-dependent translocation of SufI in the absence of cytosolic helper proteins. Biochemistry 48: 5096-5105.
    • (2009) Biochemistry , vol.48 , pp. 5096-5105
    • Holzapfel, E.1    Moser, M.2    Schiltz, E.3    Ueda, T.4    Betton, J.M.5
  • 19
    • 23244445172 scopus 로고    scopus 로고
    • Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins
    • DOI 10.1021/bp049553u
    • Kuruma Y, Nishiyama KI, Shimizu Y, Müller M, Ueda T (2005) Development of a Minimal Cell-Free Translation System for the Synthesis of Presecretory and Integral Membrane Proteins. Biotechnol Prog 21: 1243-1251. (Pubitemid 41099597)
    • (2005) Biotechnology Progress , vol.21 , Issue.4 , pp. 1243-1251
    • Kuruma, Y.1    Nishiyama, K.-I.2    Shimizu, Y.3    Muller, M.4    Ueda, T.5
  • 20
    • 77950518678 scopus 로고    scopus 로고
    • A novel complete reconstitution system for membrane integration of the simplest membrane protein
    • Nishiyama K, Maeda M, Abe M, Kanamori T, Shimamoto K, et al. (2010) A novel complete reconstitution system for membrane integration of the simplest membrane protein. Biochem Biophys Res Commun 394: 733-736.
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 733-736
    • Nishiyama, K.1    Maeda, M.2    Abe, M.3    Kanamori, T.4    Shimamoto, K.5
  • 21
    • 0032816265 scopus 로고    scopus 로고
    • In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein- targeting pathways of Escherichia coli
    • Koch HG, Hengelage T, Neumann-Haefelin C, MacFarlane J, Hoffschulte HK, et al. (1999) In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent proteintargeting pathways of Escherichia coli. Mol Biol Cell 10: 2163-2173. (Pubitemid 29343126)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.7 , pp. 2163-2173
    • Koch, H.-G.1    Hengelage, T.2    Neumann-Haefelin, C.3    MacFarlane, J.4    Hoffschulte, H.K.5    Schimz, K.-L.6    Mechler, B.7    Muller, M.8
  • 22
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. Coli
    • Young TS, Ahmad I, Yin JA, Schultz PG (2010) An enhanced system for unnatural amino acid mutagenesis in E. coli. J Mol Biol 395: 361-374.
    • (2010) J Mol Biol , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 24
    • 0034602846 scopus 로고    scopus 로고
    • Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
    • Beck K, Wu LF, Brunner J, Müller M (2000) Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J 19: 134-143. (Pubitemid 30009233)
    • (2000) EMBO Journal , vol.19 , Issue.1 , pp. 134-143
    • Beck, K.1    Wu, L.-F.2    Brunner, J.3    Muller, M.4
  • 25
    • 79251576465 scopus 로고    scopus 로고
    • SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria
    • Huber D, Rajagopalan N, Preissler S, Rocco MA, Merz F, et al. (2011) SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria. Mol Cell 41: 343-353.
    • (2011) Mol Cell , vol.41 , pp. 343-353
    • Huber, D.1    Rajagopalan, N.2    Preissler, S.3    Rocco, M.A.4    Merz, F.5
  • 27
    • 79953737877 scopus 로고    scopus 로고
    • The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon
    • Kuhn P, Weiche B, Sturm L, Sommer E, Drepper F, et al. (2011) The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon. Traffic 12: 563-578.
    • (2011) Traffic , vol.12 , pp. 563-578
    • Kuhn, P.1    Weiche, B.2    Sturm, L.3    Sommer, E.4    Drepper, F.5
  • 28
    • 0026613981 scopus 로고
    • Evolutionary conserved nucleotides within the E.Coli 4.5S RNA are required for association with P48 in vitro and for optimal function in vivo
    • Wood H, Luirink J, Tollervey D (1992) Evolutionary conserved nucleotides within the E.coli 4.5S RNA are required for association with P48 in vitro and for optimal function in vivo. Nucleic Acids Res 20: 5919-5925.
    • (1992) Nucleic Acids Res , vol.20 , pp. 5919-5925
    • Wood, H.1    Luirink, J.2    Tollervey, D.3
  • 29
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. Coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, et al. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12: 291-299.
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5
  • 30
    • 0016205087 scopus 로고
    • Isolation and partial characterization of Escherichia coli mutants with low levels of transfer ribonucleic acid nucleotidyltransferase
    • Deutscher MP, Hilderman RH (1974) Isolation and partial characterization of Escherichia coli mutants with low levels of transfer ribonucleic acid nucleotidyltransferase. J Bacteriol 118: 621-627.
    • (1974) J Bacteriol , vol.118 , pp. 621-627
    • Deutscher, M.P.1    Hilderman, R.H.2
  • 31
    • 36549072024 scopus 로고    scopus 로고
    • In vitro analysis of the bacterial twin-arginine-dependent protein export
    • Moser M, Panahandeh S, Holzapfel E, Müller M (2007) In vitro analysis of the bacterial twin-arginine-dependent protein export. Methods Mol Biol 390: 63-80.
    • (2007) Methods Mol Biol , vol.390 , pp. 63-80
    • Moser, M.1    Panahandeh, S.2    Holzapfel, E.3    Müller, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.