메뉴 건너뛰기




Volumn 24, Issue 12, 2016, Pages 2092-2101

Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy

Author keywords

cryo EM; mixing spraying; recycling; ribosome; time resolved

Indexed keywords

ELONGATION FACTOR G; ESCHERICHIA COLI PROTEIN; MESSENGER RNA; P SITE BOUND TRANSFER RNA; RIBOSOME RECYCLING FACTOR; TRANSFER RNA; UNCLASSIFIED DRUG; GUANOSINE TRIPHOSPHATE; PROTEIN BINDING; RIBOSOME PROTEIN;

EID: 85002291937     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.09.014     Document Type: Article
Times cited : (68)

References (45)
  • 2
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen, G.S., Zavialov, A., Gursky, R., Ehrenberg, M., Frank, J., The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121 (2005), 703–712.
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 3
    • 34447331273 scopus 로고    scopus 로고
    • Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits
    • Barat, C., Datta, P.P., Raj, V.S., Sharma, M.R., Kaji, H., Kaji, A., Agrawal, R.K., Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits. Mol. Cell 27 (2007), 250–261.
    • (2007) Mol. Cell , vol.27 , pp. 250-261
    • Barat, C.1    Datta, P.P.2    Raj, V.S.3    Sharma, M.R.4    Kaji, H.5    Kaji, A.6    Agrawal, R.K.7
  • 4
    • 85009829571 scopus 로고    scopus 로고
    • Complete kinetic mechanism for recycling of the bacterial ribosome
    • Borg, A., Pavlov, M., Ehrenberg, M., Complete kinetic mechanism for recycling of the bacterial ribosome. RNA 22 (2016), 10–21.
    • (2016) RNA , vol.22 , pp. 10-21
    • Borg, A.1    Pavlov, M.2    Ehrenberg, M.3
  • 6
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S., McMullan, G., Faruqi, A.R., Murshudov, G.N., Short, J.M., Scheres, S.H.W., Henderson, R., High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135 (2013), 24–35.
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1    McMullan, G.2    Faruqi, A.R.3    Murshudov, G.N.4    Short, J.M.5    Scheres, S.H.W.6    Henderson, R.7
  • 7
    • 84930273910 scopus 로고    scopus 로고
    • Structural dynamics of ribosome subunit association studied by mixing-spraying time-resolved cryogenic electron microscopy
    • Chen, B., Kaledhonkar, S., Sun, M., Shen, B., Lu, Z., Barnard, D., Lu, T.-M., Gonzalez, Ruben L. Jr., Frank, J., Structural dynamics of ribosome subunit association studied by mixing-spraying time-resolved cryogenic electron microscopy. Structure 23 (2015), 1097–1105.
    • (2015) Structure , vol.23 , pp. 1097-1105
    • Chen, B.1    Kaledhonkar, S.2    Sun, M.3    Shen, B.4    Lu, Z.5    Barnard, D.6    Lu, T.-M.7    Gonzalez, R.L.8    Frank, J.9
  • 8
    • 0034759978 scopus 로고    scopus 로고
    • Interaction of translation initiation factor 3 with the 30S ribosomal subunit
    • Dallas, A., Noller, H.F., Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol. Cell 8 (2001), 855–864.
    • (2001) Mol. Cell , vol.8 , pp. 855-864
    • Dallas, A.1    Noller, H.F.2
  • 11
    • 77954650144 scopus 로고    scopus 로고
    • Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    • Fischer, N., Konevega, A.L., Wintermeyer, W., Rodnina, M.V., Stark, H., Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy. Nature 466 (2010), 329–333.
    • (2010) Nature , vol.466 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Wintermeyer, W.3    Rodnina, M.V.4    Stark, H.5
  • 12
    • 0033009527 scopus 로고    scopus 로고
    • Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C-terminal modulator element
    • Fujiwara, T., Ito, K., Nakayashiki, T., Nakamura, Y., Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C-terminal modulator element. FEBS Lett. 447 (1999), 297–302.
    • (1999) FEBS Lett. , vol.447 , pp. 297-302
    • Fujiwara, T.1    Ito, K.2    Nakayashiki, T.3    Nakamura, Y.4
  • 13
    • 20444430084 scopus 로고    scopus 로고
    • Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies
    • Gao, N., Zavialov, A.V., Li, W., Sengupta, J., Valle, M., Gursky, R.P., Ehrenberg, M., Frank, J., Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies. Mol. Cell 18 (2005), 663–674.
    • (2005) Mol. Cell , vol.18 , pp. 663-674
    • Gao, N.1    Zavialov, A.V.2    Li, W.3    Sengupta, J.4    Valle, M.5    Gursky, R.P.6    Ehrenberg, M.7    Frank, J.8
  • 14
    • 36249001733 scopus 로고    scopus 로고
    • Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits
    • Gao, N., Zavialov, A.V., Ehrenberg, M., Frank, J., Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits. J. Mol. Biol. 374 (2007), 1345–1358.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1345-1358
    • Gao, N.1    Zavialov, A.V.2    Ehrenberg, M.3    Frank, J.4
  • 15
    • 39149091041 scopus 로고    scopus 로고
    • Preparation of macromolecular complexes for cryo-electron microscopy
    • Grassucci, R.A., Taylor, D.J., Frank, J., Preparation of macromolecular complexes for cryo-electron microscopy. Nat. Protoc. 2 (2007), 3239–3246.
    • (2007) Nat. Protoc. , vol.2 , pp. 3239-3246
    • Grassucci, R.A.1    Taylor, D.J.2    Frank, J.3
  • 16
    • 0015887427 scopus 로고
    • Role of elongation factor g and a protein factor on the release of ribosomes from messenger ribonucleic acid
    • Hirashima, A., Kaji, A., Role of elongation factor g and a protein factor on the release of ribosomes from messenger ribonucleic acid. J. Biol. Chem. 248 (1973), 7580–7587.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7580-7587
    • Hirashima, A.1    Kaji, A.2
  • 18
    • 0036296507 scopus 로고    scopus 로고
    • Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains
    • Ito, K., Fujiwara, T., Toyoda, T., Nakamura, Y., Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains. Mol. Cell 9 (2002), 1263–1272.
    • (2002) Mol. Cell , vol.9 , pp. 1263-1272
    • Ito, K.1    Fujiwara, T.2    Toyoda, T.3    Nakamura, Y.4
  • 19
    • 79960917084 scopus 로고    scopus 로고
    • The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli
    • Julián, P., Milon, P., Agirrezabala, X., Lasso, G., Gil, D., Rodnina, M.V., Valle, M., The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS Biol., 9, 2011, e1001095.
    • (2011) PLoS Biol. , vol.9 , pp. e1001095
    • Julián, P.1    Milon, P.2    Agirrezabala, X.3    Lasso, G.4    Gil, D.5    Rodnina, M.V.6    Valle, M.7
  • 20
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi, R., Pavlov, M.Y., Buckingham, R.H., Ehrenberg, M., Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell 3 (1999), 601–609.
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 21
    • 0343618468 scopus 로고    scopus 로고
    • Crystal structure of the ribosome recycling factor from Escherichia coli
    • Kim, K.K., Min, K., Suh, S.W., Crystal structure of the ribosome recycling factor from Escherichia coli. EMBO J. 19 (2000), 2362–2370.
    • (2000) EMBO J. , vol.19 , pp. 2362-2370
    • Kim, K.K.1    Min, K.2    Suh, S.W.3
  • 22
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • Lancaster, L., Kiel, M.C., Kaji, A., Noller, H.F., Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell 111 (2002), 129–140.
    • (2002) Cell , vol.111 , pp. 129-140
    • Lancaster, L.1    Kiel, M.C.2    Kaji, A.3    Noller, H.F.4
  • 23
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enables near atomic resolution single particle cryoEM
    • Li, X., Mooney, P., Zheng, S., Booth, C., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y., Electron counting and beam-induced motion correction enables near atomic resolution single particle cryoEM. Nat. Methods 10 (2013), 584–590.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 27
    • 47049098691 scopus 로고    scopus 로고
    • Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting
    • Pavlov, M.Y., Antoun, A., Lovmar, M., Ehrenberg, M., Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting. EMBO J. 27 (2008), 1706–1717.
    • (2008) EMBO J. , vol.27 , pp. 1706-1717
    • Pavlov, M.Y.1    Antoun, A.2    Lovmar, M.3    Ehrenberg, M.4
  • 30
    • 84864479919 scopus 로고    scopus 로고
    • Structure and mechanical properties of the ribosomal L1 stalk three-way junction
    • Réblová, K., Šponer, J., Lankaš, F., Structure and mechanical properties of the ribosomal L1 stalk three-way junction. Nucleic Acids Res. 40 (2012), 6290–6303.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 6290-6303
    • Réblová, K.1    Šponer, J.2    Lankaš, F.3
  • 31
    • 13944279104 scopus 로고    scopus 로고
    • Interaction of RRF and EF-G from E. coli and T. thermophilus with ribosomes from both origins—insight into the mechanism of the ribosome recycling step
    • Raj, V.S., Kaji, H., Kaji, A., Interaction of RRF and EF-G from E. coli and T. thermophilus with ribosomes from both origins—insight into the mechanism of the ribosome recycling step. RNA 11 (2005), 275–284.
    • (2005) RNA , vol.11 , pp. 275-284
    • Raj, V.S.1    Kaji, H.2    Kaji, A.3
  • 32
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V., Ribosome structure and the mechanism of translation. Cell 108 (2002), 557–572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 33
    • 65249164177 scopus 로고    scopus 로고
    • Distinct functions of elongation factor G in ribosome recycling and translocation
    • Savelsbergh, A., Rodnina, M.V., Wintermeyer, W., Distinct functions of elongation factor G in ribosome recycling and translocation. RNA 15 (2009), 772–780.
    • (2009) RNA , vol.15 , pp. 772-780
    • Savelsbergh, A.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 34
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H.W., RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180 (2012), 519–530.
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 35
    • 0142178293 scopus 로고    scopus 로고
    • Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit
    • Schmeing, T.M., Moore, P.B., Steitz, T.A., Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA 9 (2003), 1345–1352.
    • (2003) RNA , vol.9 , pp. 1345-1352
    • Schmeing, T.M.1    Moore, P.B.2    Steitz, T.A.3
  • 36
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic
    • Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A., Liljas, A., Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science 286 (1999), 2349–2352.
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirokawa, G.3    Kaji, A.4    Liljas, A.5
  • 37
  • 39
    • 0033751564 scopus 로고    scopus 로고
    • Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch
    • Toyoda, T., Tin, O.F., Ito, K., Fujiwara, T., Kumasaka, T., Yamamoto, M., Garber, M.B., Nakamura, Y., Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch. RNA 6 (2000), 1432–1444.
    • (2000) RNA , vol.6 , pp. 1432-1444
    • Toyoda, T.1    Tin, O.F.2    Ito, K.3    Fujiwara, T.4    Kumasaka, T.5    Yamamoto, M.6    Garber, M.B.7    Nakamura, Y.8
  • 41
    • 13444306224 scopus 로고    scopus 로고
    • X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit
    • Wilson, D.N., Schluenzen, F., Harms, J.M., Yoshida, T., Ohkubo, T., Albrecht, R., Buerger, J., Kobayashi, Y., Fucini, P., X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit. EMBO J. 24 (2004), 251–260.
    • (2004) EMBO J. , vol.24 , pp. 251-260
    • Wilson, D.N.1    Schluenzen, F.2    Harms, J.M.3    Yoshida, T.4    Ohkubo, T.5    Albrecht, R.6    Buerger, J.7    Kobayashi, Y.8    Fucini, P.9
  • 42
    • 84859432765 scopus 로고    scopus 로고
    • Structural insights into initial and intermediate steps of the ribosome-recycling process
    • Yokoyama, T., Shaikh, T.R., Iwakura, N., Kaji, H., Kaji, A., Agrawal, R.K., Structural insights into initial and intermediate steps of the ribosome-recycling process. EMBO J. 31 (2012), 1836–1846.
    • (2012) EMBO J. , vol.31 , pp. 1836-1846
    • Yokoyama, T.1    Shaikh, T.R.2    Iwakura, N.3    Kaji, H.4    Kaji, A.5    Agrawal, R.K.6
  • 43
    • 0037446515 scopus 로고    scopus 로고
    • Characteristic domain motion in the ribosome recycling factor revealed by 15N NMR relaxation experiments and molecular dynamics simulations
    • Yoshida, T., Oka, S., Uchiyama, S., Nakano, H., Kawasaki, T., Ohkubo, T., Kobayashi, Y., Characteristic domain motion in the ribosome recycling factor revealed by 15N NMR relaxation experiments and molecular dynamics simulations. Biochemistry 42 (2003), 4101–4107.
    • (2003) Biochemistry , vol.42 , pp. 4101-4107
    • Yoshida, T.1    Oka, S.2    Uchiyama, S.3    Nakano, H.4    Kawasaki, T.5    Ohkubo, T.6    Kobayashi, Y.7
  • 45
    • 20444420154 scopus 로고    scopus 로고
    • Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G
    • Zavialov, A.V., Hauryliuk, V.V., Ehrenberg, M., Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G. Mol. Cell 18 (2005), 675–686.
    • (2005) Mol. Cell , vol.18 , pp. 675-686
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.