메뉴 건너뛰기




Volumn 18, Issue 6, 2005, Pages 663-674

Mechanism for the disassembly of the posttermination complex inferred from Cryo-EM studies

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; MESSENGER RNA; RIBOSOME RECYCLING FACTOR;

EID: 20444430084     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.05.005     Document Type: Article
Times cited : (105)

References (56)
  • 1
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
    • R.K. Agrawal, P. Penczek, R.A. Grassucci, and J. Frank Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation Proc. Natl. Acad. Sci. USA 95 1998 6134 6138
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Frank, J.4
  • 2
    • 0032967391 scopus 로고    scopus 로고
    • Conformational variability in Escherichia coli 70S ribosome as revealed by 3D cryo-electron microscopy
    • R.K. Agrawal, R.K. Lata, and J. Frank Conformational variability in Escherichia coli 70S ribosome as revealed by 3D cryo-electron microscopy Int. J. Biochem. Cell Biol. 31 1999 243 254
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 243-254
    • Agrawal, R.K.1    Lata, R.K.2    Frank, J.3
  • 3
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • R.K. Agrawal, A.B. Heagle, P. Penczek, R.A. Grassucci, and J. Frank EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome Nat. Struct. Biol. 7 1999 643 647
    • (1999) Nat. Struct. Biol. , vol.7 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 5
    • 0035957387 scopus 로고    scopus 로고
    • A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit
    • L. Belova, T. Tenson, L. Xiong, P.M. McNicholas, and A.S. Mankin A novel site of antibiotic action in the ribosome: interaction of evernimicin with the large ribosomal subunit Proc. Natl. Acad. Sci. USA 98 2001 3726 3731
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3726-3731
    • Belova, L.1    Tenson, T.2    Xiong, L.3    McNicholas, P.M.4    Mankin, A.S.5
  • 7
    • 0042173407 scopus 로고    scopus 로고
    • Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex
    • A.R. Cukras, D.R. Southworth, J.L. Brunelle, G.M. Culver, and R. Green Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex Mol. Cell 12 2003 321 328
    • (2003) Mol. Cell , vol.12 , pp. 321-328
    • Cukras, A.R.1    Southworth, D.R.2    Brunelle, J.L.3    Culver, G.M.4    Green, R.5
  • 8
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • J. Frank, and R.K. Agrawal A ratchet-like inter-subunit reorganization of the ribosome during translocation Nature 406 2000 318 322
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 9
    • 0035787732 scopus 로고    scopus 로고
    • Ratchet-like movement between the two ribosomal subunits: Their implications in elongation factor recognition and tRNA translocation
    • J. Frank, and R.K. Agrawal Ratchet-like movement between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation Cold Spring Harb. Symp. Quant. Biol. 66 2001 67 75
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 67-75
    • Frank, J.1    Agrawal, R.K.2
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 12
    • 3242876203 scopus 로고    scopus 로고
    • Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor G
    • T. Fujiwara, K. Ito, T. Yamami, and Y. Nakamura Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor G Mol. Microbiol. 53 2004 517 528
    • (2004) Mol. Microbiol. , vol.53 , pp. 517-528
    • Fujiwara, T.1    Ito, K.2    Yamami, T.3    Nakamura, Y.4
  • 15
    • 4344605740 scopus 로고    scopus 로고
    • Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset
    • H. Gao, M. Valle, M. Ehrenberg, and J. Frank Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset J. Struct. Biol. 147 2004 283 290
    • (2004) J. Struct. Biol. , vol.147 , pp. 283-290
    • Gao, H.1    Valle, M.2    Ehrenberg, M.3    Frank, J.4
  • 16
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • C.O. Gualerzi, and C.L. Pon Initiation of mRNA translation in prokaryotes Biochemistry 29 1990 5881 5889
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 17
    • 0015887427 scopus 로고
    • Role of elongation factor G and a protein factor on the release of ribosomes from messenger ribonucleic acid
    • A. Hirashima, and A. Kaji 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
  • 20
    • 0036296507 scopus 로고    scopus 로고
    • Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains
    • K. Ito, T. Fujiwara, T. Toyoda, and Y. Nakamura 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
  • 21
    • 0028314657 scopus 로고
    • Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth
    • L. Janosi, I. Shimizu, and A. Kaji Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth Proc. Natl. Acad. Sci. USA 91 1994 4249 4253
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4249-4253
    • Janosi, L.1    Shimizu, I.2    Kaji, A.3
  • 22
    • 0029950071 scopus 로고    scopus 로고
    • Ribosome recycling by ribosome recycling factor (RRF) - An important but overlooked step of protein biosynthesis
    • L. Janosi, H. Hara, S. Zhang, and A. Kaji Ribosome recycling by ribosome recycling factor (RRF) - an important but overlooked step of protein biosynthesis Adv. Biophys. 32 1996 121 201
    • (1996) Adv. Biophys. , vol.32 , pp. 121-201
    • Janosi, L.1    Hara, H.2    Zhang, S.3    Kaji, A.4
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and N.O. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. 47 1991 110 119
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, N.O.4
  • 25
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • R. Karimi, M.Y. Pavlov, R.H. Buckingham, and M. Ehrenberg 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
  • 26
    • 0346850831 scopus 로고    scopus 로고
    • Release of ribosome-bound ribosome recycling factor by elongation factor G
    • M.C. Kiel, V.S. Raj, H. Kaji, and A. Kaji Release of ribosome-bound ribosome recycling factor by elongation factor G J. Biol. Chem. 278 2003 48041 48050
    • (2003) J. Biol. Chem. , vol.278 , pp. 48041-48050
    • Kiel, M.C.1    Raj, V.S.2    Kaji, H.3    Kaji, A.4
  • 27
    • 0343618468 scopus 로고    scopus 로고
    • Crystal structure of the ribosome recycling factor from Escherichia coli
    • K.K. Kim, K. Min, and S.W. Suh 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
  • 28
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • L. Lancaster, M.C. Kiel, A. Kaji, and H.F. Noller 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
  • 31
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • D. Moazed, and H.F. Noller Intermediate states in the movement of transfer RNA in the ribosome Nature 342 1989 142 148
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 32
    • 0025642374 scopus 로고
    • Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly
    • M. Moritz, A.G. Paulovich, Y.F. Tsay, and J.L. Woolford Jr. Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly J. Cell Biol. 111 1990 2261 2274
    • (1990) J. Cell Biol. , vol.111 , pp. 2261-2274
    • Moritz, M.1    Paulovich, A.G.2    Tsay, Y.F.3    Woolford Jr., J.L.4
  • 34
    • 18944364304 scopus 로고    scopus 로고
    • Sequence of steps in ribosome recycling as defined by kinetic analysis
    • F. Peske, M.V. Rodnina, and W. Wintermeyer Sequence of steps in ribosome recycling as defined by kinetic analysis Mol. Cell 18 2005 403 412
    • (2005) Mol. Cell , vol.18 , pp. 403-412
    • Peske, F.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 35
    • 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
    • V.S. Raj, H. Kaji, and A. Kaji 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
  • 36
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome Structure and the Mechanism of Translation
    • V. Ramakrishnan Ribosome Structure and the Mechanism of Translation Cell 108 2002 557 572
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 37
    • 0035355353 scopus 로고    scopus 로고
    • Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediates peptidyl-tRNA release and ribosome recycling in Escherichia coli
    • A.R. Rao, and U. Varshney Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediates peptidyl-tRNA release and ribosome recycling in Escherichia coli EMBO J. 20 2001 2977 2986
    • (2001) EMBO J. , vol.20 , pp. 2977-2986
    • Rao, A.R.1    Varshney, U.2
  • 38
    • 0036953086 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome
    • A.R. Rao, and U. Varshney Characterization of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome Microbiol. 148 2002 3913 3920
    • (2002) Microbiol. , vol.148 , pp. 3913-3920
    • Rao, A.R.1    Varshney, U.2
  • 39
    • 9644260557 scopus 로고    scopus 로고
    • X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications
    • K. Saikrishnan, S.K. Kalapala, U. Varshney, and M. Vijayan X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications J. Mol. Biol. 345 2005 29 38
    • (2005) J. Mol. Biol. , vol.345 , pp. 29-38
    • Saikrishnan, K.1    Kalapala, S.K.2    Varshney, U.3    Vijayan, M.4
  • 40
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic
    • M. Selmer, S. Al-Karadaghi, G. Hirokawa, A. Kaji, and A. Liljas 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
  • 41
    • 4944227490 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of RRF, EF-G, and thiostrepton interaction on the Escherichia coli ribosome
    • H.S. Seo, M. Kiel, D. Pan, V.S. Raj, A. Kaji, and B.S. Cooperman Kinetics and thermodynamics of RRF, EF-G, and thiostrepton interaction on the Escherichia coli ribosome Biochemistry 43 2004 12728 12740
    • (2004) Biochemistry , vol.43 , pp. 12728-12740
    • Seo, H.S.1    Kiel, M.2    Pan, D.3    Raj, V.S.4    Kaji, A.5    Cooperman, B.S.6
  • 42
    • 0037029091 scopus 로고    scopus 로고
    • Ribosome as a molecular machine
    • A.S. Spirin Ribosome as a molecular machine FEBS Lett. 514 2002 2 10
    • (2002) FEBS Lett. , vol.514 , pp. 2-10
    • Spirin, A.S.1
  • 43
    • 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
    • T. Toyoda, O.F. Tin, K. Ito, T. Fujiwara, T. Kumasaka, M. Yamamoto, M.B. Garber, and Y. Nakamura 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
  • 46
    • 0034624039 scopus 로고    scopus 로고
    • Movement of the decoding region of the 16 S ribosomal RNA accompanies tRNA translocation
    • M.S. VanLoock, R.K. Agrawal, I.S. Gabashvili, L. Qi, J. Frank, and S.C. Harvey Movement of the decoding region of the 16 S ribosomal RNA accompanies tRNA translocation J. Mol. Biol. 304 2000 507 515
    • (2000) J. Mol. Biol. , vol.304 , pp. 507-515
    • Vanloock, M.S.1    Agrawal, R.K.2    Gabashvili, I.S.3    Qi, L.4    Frank, J.5    Harvey, S.C.6
  • 48
    • 12344317358 scopus 로고    scopus 로고
    • Heterologous expression of Aquifex aeolicus ribosome recycling factor in Escherichia coli is dominant lethal by forming a complex that lacks functional co-ordination for ribosome disassembly
    • T. Yamami, K. Ito, T. Fujiwara, and Y. Nakamura Heterologous expression of Aquifex aeolicus ribosome recycling factor in Escherichia coli is dominant lethal by forming a complex that lacks functional co-ordination for ribosome disassembly Mol. Microbiol. 55 2005 150 161
    • (2005) Mol. Microbiol. , vol.55 , pp. 150-161
    • Yamami, T.1    Ito, K.2    Fujiwara, T.3    Nakamura, Y.4
  • 50
    • 0037446515 scopus 로고    scopus 로고
    • Characteristic domain motion in the ribosome recycling factor revealed by 15N NMR relaxation experiments and molecular dynamics simulations
    • T. Yoshida, S. Oka, S. Uchiyama, H. Nakano, T. Kawasaki, T. Ohkubo, and Y. Kobayashi 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
  • 52
    • 0038300651 scopus 로고    scopus 로고
    • Peptidyl-tRNA regulates the GTPase activity of translation factors
    • A.V. Zavialov, and M. Ehrenberg Peptidyl-tRNA regulates the GTPase activity of translation factors Cell 114 2003 113 122
    • (2003) Cell , vol.114 , pp. 113-122
    • Zavialov, A.V.1    Ehrenberg, M.2
  • 53
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • A.V. Zavialov, R.H. Buckingham, and M. Ehrenberg A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3 Cell 107 2001 115 124
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 54
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • A.V. Zavialov, L. Mora, R.H. Buckingham, and M. Ehrenberg Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3 Mol. Cell 10 2002 789 798
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 55
    • 20444420154 scopus 로고    scopus 로고
    • Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G
    • Published online June 2, 2005. 10.1016/S1097276505013420.
    • Zavialov, A.V., Hauryliuk, V.V., and Ehrenberg, M. (2005a). Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G. Mol. Cell 18, this issue, 675-686. Published online June 2, 2005. 10.1016/S1097276505013420.
    • (2005) Mol. Cell , vol.18 , Issue.THIS ISSUE , pp. 675-686
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3
  • 56
    • 20444393817 scopus 로고    scopus 로고
    • Guanine nucleotide exchange on ribosome bound elongation factor G initiates translocation of tRNAs
    • in press.
    • Zavialov, A.V., Hauryliuk, V.V. and Ehrenberg, M. (2005b). Guanine nucleotide exchange on ribosome bound elongation factor G initiates translocation of tRNAs. J. Biol., in press.
    • (2005) J. Biol.
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.