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Volumn 492, Issue 7428, 2012, Pages 271-275

Activated GTPase movement on an RNA scaffold drives co-translational protein targeting

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PROTEIN SECYEG; PROTEOME; RIBONUCLEOPROTEIN; RNA; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 84870979537     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11726     Document Type: Article
Times cited : (64)

References (38)
  • 2
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • Pool, M. R., Stumm, J., Fulga, T. A., Sinning, I. & Dobberstein, B. Distinct modes of signal recognition particle interaction with the ribosome. Science 297, 1345-1348 (2002).
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 3
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic, M. et al. Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 444, 507-511 (2006).
    • (2006) Nature , vol.444 , pp. 507-511
    • Halic, M.1
  • 4
    • 33751325833 scopus 로고    scopus 로고
    • Structure of the E. coli signal recognition particle bound to a translating ribosome
    • Schaffitzel, C. et al. Structure of the E. coli signal recognition particle bound to a translating ribosome. Nature 444, 503-506 (2006).
    • (2006) Nature , vol.444 , pp. 503-506
    • Schaffitzel, C.1
  • 6
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • Egea, P. F. et al. Substrate twinning activates the signal recognition particle and its receptor. Nature 427, 215-221 (2004).
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1
  • 7
    • 71549167617 scopus 로고    scopus 로고
    • Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome
    • Becker, T. et al. Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science 326, 1369-1373 (2009).
    • (2009) Science , vol.326 , pp. 1369-1373
    • Becker, T.1
  • 8
    • 0035909810 scopus 로고    scopus 로고
    • Role of SRP RNA in the GTPase cycles of ffh and FtsY
    • Peluso, P., Shan, S. O., Nock, S., Herschlag, D. & Walter, P. Role of SRP RNA in the GTPase cycles of ffh and FtsY. Biochemistry 40, 15224-15233 (2001).
    • (2001) Biochemistry , vol.40 , pp. 15224-15233
    • Peluso, P.1    Shan, S.O.2    Nock, S.3    Herschlag, D.4    Walter, P.5
  • 9
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang, X., Rashid, R., Wang, K. & Shan, S. O. Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 328, 757-760 (2010).
    • (2010) Science , vol.328 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.O.4
  • 10
    • 77953025666 scopus 로고    scopus 로고
    • Recognition of a signal peptide by the signal recognition particle
    • Janda, C. Y. et al. Recognition of a signal peptide by the signal recognition particle. Nature 465, 507-510 (2010).
    • (2010) Nature , vol.465 , pp. 507-510
    • Janda, C.Y.1
  • 11
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey, R. T., Rambo, R. P., Lucast, L., Rha, B. & Doudna, J. A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287,1232-1239 (2000).
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 12
    • 47849117948 scopus 로고    scopus 로고
    • Demonstration of a multistep mechanism for assembly of the SRP?SRP receptor complex: Implications for the catalytic role of SRP RNA
    • Zhang, X., Kung, S. & Shan, S. O. Demonstration of a multistep mechanism for assembly of the SRP?SRP receptor complex: implications for the catalytic role of SRP RNA. J. Mol. Biol. 381, 581-593 (2008).
    • (2008) J. Mol. Biol , vol.381 , pp. 581-593
    • Zhang, X.1    Kung, S.2    Shan, S.O.3
  • 13
    • 77952331762 scopus 로고    scopus 로고
    • Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting
    • Shen, K. & Shan, S. O. Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting. Proc. Natl Acad. Sci. USA 107, 7698-7703 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 7698-7703
    • Shen, K.1    Shan, S.O.2
  • 14
    • 79955005771 scopus 로고    scopus 로고
    • Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting
    • Shen, K., Zhang, X. & Shan, S. O. Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting. RNA 17, 892-902 (2011).
    • (2011) RNA , vol.17 , pp. 892-902
    • Shen, K.1    Zhang, X.2    Shan, S.O.3
  • 15
    • 78650974443 scopus 로고    scopus 로고
    • Cryo-EMstructure of the E. coli translating ribosome in complex withSRP and its receptor
    • Estrozi, L. F., Boehringer, D., Shan, S., Ban, N. & Schaffitzel, C. Cryo-EMstructure of the E. coli translating ribosome in complex withSRP and its receptor. Nature Struct. Mol. Biol. 18, 88-90 (2011).
    • (2011) Nature Struct. Mol. Biol , vol.18 , pp. 88-90
    • Estrozi, L.F.1    Boehringer, D.2    Shan, S.3    Ban, N.4    Schaffitzel, C.5
  • 16
    • 0028303640 scopus 로고
    • Molecular evolution of SRP cycle components: Functional implications
    • Althoff, S., Selinger, D. & Wise, J. A. Molecular evolution of SRP cycle components: functional implications. Nucleic Acids Res. 22, 1933-1947 (1994).
    • (1994) Nucleic Acids Res , vol.22 , pp. 1933-1947
    • Althoff, S.1    Selinger, D.2    Wise, J.A.3
  • 17
    • 79951826865 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle in complex with its receptor
    • Ataide, S. F. et al. The crystal structure of the signal recognition particle in complex with its receptor. Science 331, 881-886 (2011).
    • (2011) Science , vol.331 , pp. 881-886
    • Ataide, S.F.1
  • 18
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T. et al. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA 93, 6264-6268 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6264-6268
    • Ha, T.1
  • 19
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy, R., Hohng, S. & Ha, T. A practical guide to single-molecule FRET. Nature Methods 5, 507-516 (2008).
    • (2008) Nature Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 20
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney, S. A., Joo, C.& Ha, T. Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J. 91, 1941-1951 (2006).
    • (2006) Biophys. J , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 21
    • 34547929138 scopus 로고    scopus 로고
    • Conformational changes in the GTPase modules of the signal reception particle and its initiation of protein translocation
    • Shan, S. O., Chandrasekar, S. & Walter, P. Conformational changes in the GTPase modules of the signal reception particle and its initiation of protein translocation. J. Cell Biol. 178, 611-620 (2007).
    • (2007) J. Cell Biol , vol.178 , pp. 611-620
    • Shan, S.O.1    Chandrasekar, S.2    Walter, P.3
  • 22
    • 8844253060 scopus 로고    scopus 로고
    • Mechanism of association and reciprocal activation of two GTPases
    • Shan, S. O., Stroud, R. M. & Walter, P. Mechanism of association and reciprocal activation of two GTPases. PLoS Biol. 2, e320 (2004).
    • (2004) PLoS Biol , vol.2
    • Shan, S.O.1    Stroud, R.M.2    Walter, P.3
  • 23
    • 60549083291 scopus 로고    scopus 로고
    • Multiple conformational switches in a GTPase complex control co-translational protein targeting
    • Zhang, X., Schaffitzel, C.,Ban, N.&Shan,S. O.Multiple conformational switches in a GTPase complex control co-translational protein targeting. Proc. Natl Acad. Sci. USA 106, 1754-1759 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1754-1759
    • Zhang, X.1    Schaffitzel, C.2    Ban, N.3    Shan, S.O.4
  • 24
    • 79955585362 scopus 로고    scopus 로고
    • Direct visualization reveals dynamics of a transient intermediate during protein assembly
    • Zhang, X. et al. Direct visualization reveals dynamics of a transient intermediate during protein assembly. Proc. Natl Acad. Sci. USA 108, 6450-6455 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 6450-6455
    • Zhang, X.1
  • 25
    • 33646442605 scopus 로고    scopus 로고
    • Signal recognition particle receptor exposes the ribosomal translocon binding site
    • Halic, M. et al. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science 312, 745-747 (2006).
    • (2006) Science , vol.312 , pp. 745-747
    • Halic, M.1
  • 26
    • 83055184248 scopus 로고    scopus 로고
    • New insights into the spliceosome by single molecule fluorescence microscopy
    • Hoskins, A. A., Gelles, J. & Moore, M. J. New insights into the spliceosome by single molecule fluorescence microscopy. Curr. Opin. Chem. Biol. 15, 864-870 (2011).
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 864-870
    • Hoskins, A.A.1    Gelles, J.2    Moore, M.J.3
  • 27
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T. M. & Bjornson, K. P. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214 (1996).
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 28
    • 77957141376 scopus 로고    scopus 로고
    • Insight into helicase mechanism and function revealed through single-molecule approaches
    • Yodh, J. G., Schlierf, M. & Ha, T. Insight into helicase mechanism and function revealed through single-molecule approaches. Q. Rev. Biophys. 43, 185-217 (2010).
    • (2010) Q. Rev. Biophys , vol.43 , pp. 185-217
    • Yodh, J.G.1    Schlierf, M.2    Ha, T.3
  • 29
    • 0019376491 scopus 로고
    • Structure and mechanism of multifunctional restriction endonucleases
    • Yuan, R. Structure and mechanism of multifunctional restriction endonucleases. Annu. Rev. Biochem. 50, 285-315 (1981).
    • (1981) Annu. Rev. Biochem , vol.50 , pp. 285-315
    • Yuan, R.1
  • 30
    • 0034130457 scopus 로고    scopus 로고
    • Type i restriction systems: Sophisticated molecular machines (a legacy of Bertani and Weigle)
    • Murray, N. E. Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle). Microbiol. Mol. Biol. Rev. 64, 412-434 (2000).
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 31
    • 34248583785 scopus 로고    scopus 로고
    • Generation of ribosome nascent chain complexes for structural and functional studies
    • Schaffitzel, C. & Ban, N. Generation of ribosome nascent chain complexes for structural and functional studies. J. Struct. Biol. 158, 463-471 (2007).
    • (2007) J. Struct. Biol , vol.158 , pp. 463-471
    • Schaffitzel, C.1    Ban, N.2
  • 32
    • 0037063356 scopus 로고    scopus 로고
    • SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking
    • van der Sluis, E. O., Nouwen, N. & Driessen, A. J. SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking. FEBS Lett. 527, 159-165 (2002).
    • (2002) FEBS Lett , vol.527 , pp. 159-165
    • Van Der Sluis, E.O.1    Nouwen, N.2    Driessen, A.J.3
  • 33
    • 0029919746 scopus 로고    scopus 로고
    • Use of cis-andtrans-ribozymes to remove 59 and 39 heterogeneities frommilligrams of in vitro transcribed RNA
    • Ferré-D'Amaré, A. R.& Doudna, J. A. Use of cis-andtrans-ribozymes to remove 59 and 39 heterogeneities frommilligrams of in vitro transcribed RNA. Nucleic Acids Res. 24, 977-978 (1996).
    • (1996) Nucleic Acids Res , vol.24 , pp. 977-978
    • Ferré-D'Amaré, A.R.1    Doudna, J.A.2
  • 34
    • 77954733211 scopus 로고    scopus 로고
    • Reconstitution of the SecY translocon in nanodiscs
    • Dalal, K.&Duong, F. Reconstitution of the SecY translocon in nanodiscs.Methods Mol. Biol. 619, 145-156 (2010).
    • (2010) Methods Mol. Biol , vol.619 , pp. 145-156
    • Dalal, K.1    Duong, F.2
  • 35
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • Van den Berg, B. et al. X-ray structure of a protein-conducting channel. Nature 427, 36-44 (2004).
    • (2004) Nature , vol.427 , pp. 36-44
    • Van Den Berg, B.1
  • 36
    • 0032572529 scopus 로고    scopus 로고
    • Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane
    • Mothes, W., Jungnickel, B., Brunner, J. & Rapoport, T. A. Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane. J. Cell Biol. 142, 355-364 (1998).
    • (1998) J. Cell Biol , vol.142 , pp. 355-364
    • Mothes, W.1    Jungnickel, B.2    Brunner, J.3    Rapoport, T.A.4
  • 37
    • 0041736710 scopus 로고    scopus 로고
    • Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    • Duong, F. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J. 22, 4375-4384 (2003).
    • (2003) EMBO J , vol.22 , pp. 4375-4384
    • Duong, F.1
  • 38
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • Powers, T. & Walter, P. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J. 16, 4880-4886 (1997).
    • (1997) EMBO J , vol.16 , pp. 4880-4886
    • Powers, T.1    Walter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.