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Volumn 444, Issue 7118, 2006, Pages 507-511

Following the signal sequence from ribosomal tunnel exit to signal recognition particle

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; COMPLEXATION; MOLECULAR BIOLOGY; OPTICAL RESOLVING POWER; PROTEINS;

EID: 33751325296     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05326     Document Type: Article
Times cited : (169)

References (29)
  • 2
    • 8844239874 scopus 로고    scopus 로고
    • SRP-mediated protein targeting: Structure and function revisited
    • Luirink, J. & Sinning, I. SRP-mediated protein targeting: structure and function revisited. Biochim. Biophys. Acta 1694, 17-35 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 17-35
    • Luirink, J.1    Sinning, I.2
  • 3
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • Halic, M. & Beckmann, R. The signal recognition particle and its interactions during protein targeting. Curr. Opin. Struct. Biol. 15, 116-125 (2005).
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 4
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814 (2004).
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1
  • 5
    • 0038360877 scopus 로고    scopus 로고
    • Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome
    • Ullers, R. S. et al. Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome. J. Cell Biol. 161, 679-684 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 679-684
    • Ullers, R.S.1
  • 6
    • 33646042904 scopus 로고    scopus 로고
    • A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation
    • Penczek, P. A., Frank, J. & Spahn, C. M. A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation. J. Struct. Biol. 154, 184-194 (2006).
    • (2006) J. Struct. Biol. , vol.154 , pp. 184-194
    • Penczek, P.A.1    Frank, J.2    Spahn, C.M.3
  • 7
    • 0242407184 scopus 로고    scopus 로고
    • Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
    • Valle, M. et al. Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Nature Struct. Biol. 10, 899-906 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 899-906
    • Valle, M.1
  • 8
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead, C. A., McCormick, P. J. & Johnson, A. E. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116, 725-736 (2004).
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 9
    • 20444430500 scopus 로고    scopus 로고
    • Secondary structure formation of a transmembrane segment in Kv channels
    • Lu, J. & Deutsch, C. Secondary structure formation of a transmembrane segment in Kv channels. Biochemistry 44, 8230-8243 (2005).
    • (2005) Biochemistry , vol.44 , pp. 8230-8243
    • Lu, J.1    Deutsch, C.2
  • 10
    • 22244484116 scopus 로고    scopus 로고
    • Early encounters of a nascent membrane protein: Specificity and timing of contacts inside and outside the ribosome
    • Houben, E. N., Zarivach, R., Oudega, B. & Luirink, J. Early encounters of a nascent membrane protein: specificity and timing of contacts inside and outside the ribosome. J. Cell Biol. 170, 27-35 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 27-35
    • Houben, E.N.1    Zarivach, R.2    Oudega, B.3    Luirink, J.4
  • 11
    • 0038719738 scopus 로고    scopus 로고
    • Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens
    • Flanagan, J. J. et al. Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens. J. Biol. Chem. 278, 18628-18637 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 18628-18637
    • Flanagan, J.J.1
  • 12
    • 33646343968 scopus 로고    scopus 로고
    • Alternate recruitment of signal recognition particle and trigger factor to the signal sequence of a growing nascent polypeptide
    • Eisner, G., Moser, M., Schafer, U., Beck, K. & Muller, M. Alternate recruitment of signal recognition particle and trigger factor to the signal sequence of a growing nascent polypeptide. J. Biol. Chem. 281, 7172-7179 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 7172-7179
    • Eisner, G.1    Moser, M.2    Schafer, U.3    Beck, K.4    Muller, M.5
  • 13
    • 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
  • 14
    • 0344304454 scopus 로고    scopus 로고
    • Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    • Rosendal, K. R., Wild, K., Montoya, G. & Sinning, I. Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc. Natl Acad. Sci. USA 100, 14701-14706 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14701-14706
    • Rosendal, K.R.1    Wild, K.2    Montoya, G.3    Sinning, I.4
  • 15
    • 22444441692 scopus 로고    scopus 로고
    • Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET
    • Buskiewicz, I. et al. Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET. J. Mol. Biol. 351, 417-430 (2005).
    • (2005) J. Mol. Biol. , vol.351 , pp. 417-430
    • Buskiewicz, I.1
  • 16
    • 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
  • 17
    • 27644447766 scopus 로고    scopus 로고
    • The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction
    • Schlunzen, F. et al. The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction. Structure 13, 1685-1694 (2005).
    • (2005) Structure , vol.13 , pp. 1685-1694
    • Schlunzen, F.1
  • 19
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein, H. D. et al. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340, 482-486 (1989).
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1
  • 20
    • 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
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0024278072 scopus 로고
    • Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli
    • Wagenknecht, T., Grassucci, R. & Frank, J. Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli. J. Mol. Biol. 199, 137-147 (1988).
    • (1988) J. Mol. Biol. , vol.199 , pp. 137-147
    • Wagenknecht, T.1    Grassucci, R.2    Frank, J.3
  • 25
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 26
    • 27644491082 scopus 로고    scopus 로고
    • Structures of the bacterial ribosome at 3.5 Å resolution
    • Schuwirth, B. S. et al. Structures of the bacterial ribosome at 3.5 Å resolution. Science 310, 827-834 (2005).
    • (2005) Science , vol.310 , pp. 827-834
    • Schuwirth, B.S.1
  • 27
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers, W., Milligan, R. A. & McCammon, J. A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zhou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A A47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.