메뉴 건너뛰기




Volumn 17, Issue 3, 2010, Pages 313-317

α-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE; RIBOSOME RNA;

EID: 77949270274     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1756     Document Type: Article
Times cited : (165)

References (45)
  • 1
    • 0029100747 scopus 로고
    • A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome
    • Frank, J. et al. A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376, 441-444 (1995).
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1
  • 2
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P.B. & Steitz, T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289, 905-920 (2000).
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 0034636973 scopus 로고    scopus 로고
    • A comparison of the yeast and rabbit 80 S ribosome reveals the topology of the nascent chain exit tunnel, inter-subunit bridges and mammalian rRNA expansion segments
    • Morgan, D.G. et al. A comparison of the yeast and rabbit 80 S ribosome reveals the topology of the nascent chain exit tunnel, inter-subunit bridges and mammalian rRNA expansion segments. J. Mol. Biol. 301, 301-321 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 301-321
    • Morgan, D.G.1
  • 4
    • 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
  • 5
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu, J. & Deutsch, C. Electrostatics in the ribosomal tunnel modulate chain elongation rates. J. Mol. Biol. 384, 73-86 (2008).
    • (2008) J. Mol. Biol. , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 6
    • 34547569922 scopus 로고    scopus 로고
    • Mapping the electrostatic potential within the ribosomal exit tunnel
    • Lu, J., Kobertz, W.R. & Deutsch, C. Mapping the electrostatic potential within the ribosomal exit tunnel. J. Mol. Biol. 371, 1378-1391 (2007).
    • (2007) J. Mol. Biol. , vol.371 , pp. 1378-1391
    • Lu, J.1    Kobertz, W.R.2    Deutsch, C.3
  • 7
    • 0037040406 scopus 로고    scopus 로고
    • Regulatory nascent peptides in the ribosomal tunnel
    • Tenson, T. & Ehrenberg, M. Regulatory nascent peptides in the ribosomal tunnel. Cell 108, 591-594 (2002).
    • (2002) Cell , vol.108 , pp. 591-594
    • Tenson, T.1    Ehrenberg, M.2
  • 8
    • 0037072627 scopus 로고    scopus 로고
    • Instruction of translating ribosome by nascent peptide
    • Gong, F. & Yanofsky, C. Instruction of translating ribosome by nascent peptide. Science 297, 1864-1867 (2002).
    • (2002) Science , vol.297 , pp. 1864-1867
    • Gong, F.1    Yanofsky, C.2
  • 9
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. & Ito, K. The ribosomal exit tunnel functions as a discriminating gate. Cell 108, 629-636 (2002).
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 10
    • 43049089746 scopus 로고    scopus 로고
    • Molecular mechanism of drug-dependent ribosome stalling
    • Vazquez-Laslop, N., Thum, C. & Mankin, A.S. Molecular mechanism of drug-dependent ribosome stalling. Mol. Cell 30, 190-202 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 190-202
    • Vazquez-Laslop, N.1    Thum, C.2    Mankin, A.S.3
  • 11
    • 33745628037 scopus 로고    scopus 로고
    • The geometry of the ribosomal polypeptide exit tunnel
    • Voss, N.R., Gerstein, M., Steitz, T.A. & Moore, P.B. The geometry of the ribosomal polypeptide exit tunnel. J. Mol. Biol. 360, 893-906 (2006).
    • (2006) J. Mol. Biol. , vol.360 , pp. 893-906
    • Voss, N.R.1    Gerstein, M.2    Steitz, T.A.3    Moore, P.B.4
  • 13
    • 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
  • 14
    • 5144234840 scopus 로고    scopus 로고
    • Structure acquisition of the T1 domain of Kv1.3 during biogenesis
    • Kosolapov, A., Tu, L., Wang, J. & Deutsch, C. Structure acquisition of the T1 domain of Kv1.3 during biogenesis. Neuron 44, 295-307 (2004).
    • (2004) Neuron , vol.44 , pp. 295-307
    • Kosolapov, A.1    Tu, L.2    Wang, J.3    Deutsch, C.4
  • 15
    • 28544449949 scopus 로고    scopus 로고
    • Folding zones inside the ribosomal exit tunnel
    • Lu, J. & Deutsch, C. Folding zones inside the ribosomal exit tunnel. Nat. Struct. Mol. Biol. 12, 1123-1129 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1123-1129
    • Lu, J.1    Deutsch, C.2
  • 16
    • 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
  • 17
    • 33744551950 scopus 로고    scopus 로고
    • Translation arrest requires two-way communication between a nascent polypeptide and the ribosome
    • Woolhead, C.A., Johnson, A.E. & Bernstein, H.D. Translation arrest requires two-way communication between a nascent polypeptide and the ribosome. Mol. Cell 22, 587-598 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 587-598
    • Woolhead, C.A.1    Johnson, A.E.2    Bernstein, H.D.3
  • 18
    • 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
  • 19
    • 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
  • 21
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai, R., Ueda, H., Kitayama, A., Kamiya, N. & Nagamune, T. Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein Eng. 14, 529-532 (2001).
    • (2001) Protein Eng. , vol.14 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 22
    • 0029013417 scopus 로고
    • Ice-binding structure and mechanism of an antifreeze protein from winter founder
    • Sicheri, F. & Yang, D.S. Ice-binding structure and mechanism of an antifreeze protein from winter founder. Nature 375, 427-431 (1995).
    • (1995) Nature , vol.375 , pp. 427-431
    • Sicheri, F.1    Yang, D.S.2
  • 23
    • 0036177164 scopus 로고    scopus 로고
    • Solution structure of a hydrophobic analogue of the winter founder antifreeze protein
    • Liepinsh, E. et al. Solution structure of a hydrophobic analogue of the winter founder antifreeze protein. Eur. J. Biochem. 269, 1259-1266 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1259-1266
    • Liepinsh, E.1
  • 24
    • 28544452248 scopus 로고    scopus 로고
    • An induced-ft mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing, T.M., Huang, K.S., Strobel, S.A. & Steitz, T.A. An induced-ft mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438, 520-524 (2005).
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 25
    • 23044445236 scopus 로고    scopus 로고
    • Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression
    • Cruz-Vera, L.R., Rajagopal, S., Squires, C. & Yanofsky, C. Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression. Mol. Cell 19, 333-343 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 333-343
    • Cruz-Vera, L.R.1    Rajagopal, S.2    Squires, C.3    Yanofsky, C.4
  • 26
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • Kosolapov, A. & Deutsch, C. Tertiary interactions within the ribosomal exit tunnel. Nat. Struct. Mol. Biol. 16, 405-411 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 27
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H. & Johnson, A.E. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-41 (1997).
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 28
    • 60849096653 scopus 로고    scopus 로고
    • A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel
    • Berndt, U., Oellerer, S., Zhang, Y., Johnson, A.E. & Rospert, S. A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc. Natl. Acad. Sci. USA 106, 1398-1403 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1398-1403
    • Berndt, U.1    Oellerer, S.2    Zhang, Y.3    Johnson, A.E.4    Rospert, S.5
  • 29
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • Mingarro, I., Nilsson, I., Whitley, P. & von Heijne, G. Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol. 1, 3 (2000).
    • (2000) BMC Cell Biol. , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    Von Heijne, G.4
  • 30
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A.H. & Blobel, G. Cell-free translation of messenger RNA in a wheat germ system. Methods Enzymol. 96, 38-50 (1983).
    • (1983) Methods Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 31
    • 0023787021 scopus 로고
    • Direct localization of the tRNA-anticodon interaction site on the Escherichia coli 30 S ribosomal subunit by electron microscopy and computerized image averaging
    • Wagenknecht, T., Frank, J., Boublik, M., Nurse, K. & Ofengand, J. Direct localization of the tRNA-anticodon interaction site on the Escherichia coli 30 S ribosomal subunit by electron microscopy and computerized image averaging. J. Mol. Biol. 203, 753-760 (1988).
    • (1988) J. Mol. Biol. , vol.203 , pp. 753-760
    • Wagenknecht, T.1    Frank, J.2    Boublik, M.3    Nurse, K.4    Ofengand, J.5
  • 32
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J.A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 34
    • 25144458057 scopus 로고    scopus 로고
    • Sequence to structure (S2S): Display, manipulate and interconnect RNA data from sequence to structure
    • Jossinet, F. & Westhof, E. Sequence to structure (S2S): display, manipulate and interconnect RNA data from sequence to structure. Bioinformatics 21, 3320-3321 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 3320-3321
    • Jossinet, F.1    Westhof, E.2
  • 35
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer, M. et al. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313, 1935-1942 (2006).
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1
  • 36
    • 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
  • 37
    • 0032232529 scopus 로고    scopus 로고
    • MANIP: An interactive tool for modelling RNA
    • DOI 10.1016/S1093-3263(99)00010-8, PII S1093326399000108
    • Massire, C. & Westhof, E. MANIP: an interactive tool for modelling RNA. J. Mol. Graph. Model. 16, 197-205, 255-1197 (1998). (Pubitemid 30069587)
    • (1998) Journal of Molecular Graphics and Modelling , vol.16 , Issue.4-6 , pp. 197-205
    • Massire, C.1    Westhof, E.2
  • 38
    • 0043123152 scopus 로고    scopus 로고
    • Tools for the automatic identifcation and classifcation of RNA base pairs
    • Yang, H. et al. Tools for the automatic identifcation and classifcation of RNA base pairs. Nucleic Acids Res. 31, 3450-3460 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3450-3460
    • Yang, H.1
  • 39
    • 42949089487 scopus 로고    scopus 로고
    • Flexible ftting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco, L.G., Villa, E., Mitra, K., Frank, J. & Schulten, K. Flexible ftting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 40
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D.G. & Heringa, J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 41
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics 5, 5.6 (2006).
    • (2006) Curr. Protoc. Bioinformatics , vol.5 , pp. 56
    • Eswar, N.1
  • 44
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction
    • Schmeing, T.M., Huang, K.S., Kitchen, D.E., Strobel, S.A. & Steitz, T.A. Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol. Cell 20, 437-448 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 45
    • 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.