메뉴 건너뛰기




Volumn 515, Issue 7526, 2014, Pages 283-286

The complete structure of the large subunit of the mammalian mitochondrial ribosome

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDYLTRANSFERASE; RIBOSOME PROTEIN; RNA 16S; RNA 5S; TRANSFER RNA; CROSS LINKING REAGENT; MITOCHONDRIAL PROTEIN; RIBOSOME RNA;

EID: 84922065877     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13895     Document Type: Article
Times cited : (204)

References (58)
  • 1
    • 77953021899 scopus 로고    scopus 로고
    • Co-translational membrane insertion of mitochondrially encoded proteins
    • Ott, M. & Herrmann, J. M. Co-translational membrane insertion of mitochondrially encoded proteins. Biochim. Biophys. Acta 1803, 767-775 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 767-775
    • Ott, M.1    Herrmann, J.M.2
  • 2
    • 0015239528 scopus 로고
    • The general occurrence of 55 S ribosomes in mammalian liver mitochondria
    • O'Brien, T. W. The general occurrence of 55 S ribosomes in mammalian liver mitochondria. J. Biol. Chem. 246, 3409-3417 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 3409-3417
    • O'brien, T.W.1
  • 3
    • 0141953259 scopus 로고    scopus 로고
    • Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins
    • Sharma, M. R. et al. Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115, 97-108 (2003).
    • (2003) Cell , vol.115 , pp. 97-108
    • Sharma, M.R.1
  • 4
    • 78751580323 scopus 로고    scopus 로고
    • On the last common ancestor and early evolution of eukaryotes: Reconstructing the history of mitochondrial ribosomes
    • Desmond, E., Brochier-Armanet, C., Forterre, P. & Gribaldo, S. On the last common ancestor and early evolution of eukaryotes: reconstructing the history of mitochondrial ribosomes. Res. Microbiol. 162, 53-70 (2011).
    • (2011) Res. Microbiol. , vol.162 , pp. 53-70
    • Desmond, E.1    Brochier-Armanet, C.2    Forterre, P.3    Gribaldo, S.4
  • 5
    • 84897000112 scopus 로고    scopus 로고
    • Structure of the yeast mitochondrial large ribosomal subunit
    • Amunts, A. et al. Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485-1489 (2014).
    • (2014) Science , vol.343 , pp. 1485-1489
    • Amunts, A.1
  • 6
    • 84892797558 scopus 로고    scopus 로고
    • Architecture of the large subunit of the mammalian mitochondrial ribosome
    • Greber, B. J. et al. Architecture of the large subunit of the mammalian mitochondrial ribosome. Nature 505, 515-519 (2014).
    • (2014) Nature , vol.505 , pp. 515-519
    • Greber, B.J.1
  • 8
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 9
    • 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, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 10
    • 84897964300 scopus 로고    scopus 로고
    • A new system for naming ribosomal proteins
    • Ban, N. et al. A new system for naming ribosomal proteins. Curr. Opin. Struct. Biol. 24, 165-169 (2014).
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 165-169
    • Ban, N.1
  • 11
    • 84884580316 scopus 로고    scopus 로고
    • Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as newmembers of themammalian mitochondrial ribosome
    • Koc, E. C. et al. Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as newmembers of themammalian mitochondrial ribosome. Front. Physiol. 4, 183 (2013).
    • (2013) Front. Physiol. , vol.4 , pp. 183
    • Koc, E.C.1
  • 13
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4A° resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B. & Steitz, T. A. The complete atomic structure of the large ribosomal subunit at 2.4A° 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
  • 14
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer, M. & Rodnina, M. V. The ribosomal peptidyl transferase. Mol. Cell 26, 311-321 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 15
    • 66149157000 scopus 로고    scopus 로고
    • Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
    • Voorhees, R. M., Weixlbaumer, A., Loakes, D., Kelley, A. C. & Ramakrishnan, V. Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nature Struct. Mol. Biol. 16, 528-533 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 528-533
    • Voorhees, R.M.1    Weixlbaumer, A.2    Loakes, D.3    Kelley, A.C.4    Ramakrishnan, V.5
  • 16
    • 81555219350 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6
    • Klinge, S., Voigts-Hoffmann, F., Leibundgut, M., Arpagaus, S. & Ban, N. Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6. Science 334, 941-948 (2011).
    • (2011) Science , vol.334 , pp. 941-948
    • Klinge, S.1    Voigts-Hoffmann, F.2    Leibundgut, M.3    Arpagaus, S.4    Ban, N.5
  • 17
    • 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
  • 18
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlünzen, F. et al. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413, 814-821 (2001).
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlünzen, F.1
  • 20
    • 27744569528 scopus 로고    scopus 로고
    • Antibiotic susceptibility of mammalian mitochondrial translation
    • Zhang, L. et al. Antibiotic susceptibility of mammalian mitochondrial translation. FEBS Lett. 579, 6423-6427 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 6423-6427
    • Zhang, L.1
  • 21
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu, D., Blaha, G., Moore, P. B. & Steitz, T. A. Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 121, 257-270 (2005).
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 22
    • 2942571539 scopus 로고    scopus 로고
    • The comparative RNA web (CRW) site: An online database of comparative sequence and structure information for ribosomal, intron, and other RNAs
    • Cannone, J. J. et al. The comparative RNA web (CRW) site: an online database of comparative sequence and structure information for ribosomal, intron, and other RNAs. BMC Bioinform. 3, 2 (2002).
    • (2002) BMC Bioinform. , vol.3 , pp. 2
    • Cannone, J.J.1
  • 23
    • 35548996344 scopus 로고    scopus 로고
    • Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase
    • Stiburek, L. et al. Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase. J. Mol. Biol. 374, 506-516 (2007).
    • (2007) J. Mol. Biol. , vol.374 , pp. 506-516
    • Stiburek, L.1
  • 24
    • 84869389750 scopus 로고    scopus 로고
    • The YidC/Oxa1/Alb3 protein family: Common principles and distinct features
    • Saller, M. J.,Wu, Z. C., de Keyzer, J.& Driessen, A. J. M. The YidC/Oxa1/Alb3 protein family: common principles and distinct features. Biol. Chem. 393, 1279-1290 (2012).
    • (2012) Biol. Chem. , vol.393 , pp. 1279-1290
    • Saller, M.J.1    Wu, Z.C.2    De Keyzer, J.3    Driessen, A.J.M.4
  • 25
    • 84870392446 scopus 로고    scopus 로고
    • Structural aspects of mitochondrial translational apparatus
    • Agrawal, R. K. & Sharma, M. R. Structural aspects of mitochondrial translational apparatus. Curr. Opin. Struct. Biol. 22, 797-803 (2012).
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 797-803
    • Agrawal, R.K.1    Sharma, M.R.2
  • 26
    • 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
  • 27
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed, D. & Noller, H. F. Intermediate states in the movement of transfer RNA in the ribosome. Nature 342, 142-148 (1989).
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 28
    • 54049116765 scopus 로고    scopus 로고
    • Visualization of the hybrid state of tRNAbinding promoted by spontaneous ratcheting of the ribosome
    • Agirrezabala, X. et al. Visualization of the hybrid state of tRNAbinding promoted by spontaneous ratcheting of the ribosome. Mol. Cell 32, 190-197 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 190-197
    • Agirrezabala, X.1
  • 29
    • 58149191272 scopus 로고    scopus 로고
    • TRNAdb 2009: Compilation of tRNA sequences and tRNA genes
    • Jühling, F. et al. tRNAdb 2009: compilation of tRNA sequences and tRNA genes. Nucleic Acids Res. 37, D159-D162 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. D159-D162
    • Jühling, F.1
  • 30
    • 0033735040 scopus 로고    scopus 로고
    • Search for characteristic structural features of mammalian mitochondrial tRNAs
    • Helm, M. et al. Search for characteristic structural features of mammalian mitochondrial tRNAs. RNA 6, 1356-1379 (2000).
    • (2000) RNA , vol.6 , pp. 1356-1379
    • Helm, M.1
  • 32
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof local defocus and specimen tilt in electron microscopy
    • Mindell, J. A.&Grigorieff, N. Accurate determinationof 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
  • 33
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for highresolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 34
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. W. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853-854 (2012).
    • (2012) Nature Methods , vol.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 35
    • 84900435661 scopus 로고    scopus 로고
    • Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome
    • Fernández, I. S., Bai, X.-C., Murshudov, G., Scheres, S. H. W. & Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823-831 (2014).
    • (2014) Cell , vol.157 , pp. 823-831
    • Fernández, I.S.1    Bai, X.-C.2    Murshudov, G.3    Scheres, S.H.W.4    Ramakrishnan, V.5
  • 36
    • 84903739434 scopus 로고    scopus 로고
    • Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes
    • Leitner, A. et al. Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes. Proc. Natl. Acad. Sci. USA 111, 9455-9460 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 9455-9460
    • Leitner, A.1
  • 37
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • M111.014126
    • Leitner, A. et al. Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol. Cell. Proteom. 11, M111.014126 (2012).
    • (2012) Mol. Cell. Proteom. , vol.11
    • Leitner, A.1
  • 38
    • 84891714984 scopus 로고    scopus 로고
    • Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline
    • Leitner, A., Walzthoeni, T. & Aebersold, R. Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline. Nature Protocols 9, 120-137 (2014).
    • (2014) Nature Protocols , vol.9 , pp. 120-137
    • Leitner, A.1    Walzthoeni, T.2    Aebersold, R.3
  • 39
    • 84866118432 scopus 로고    scopus 로고
    • False discovery rate estimation for cross-linked peptides identified by mass spectrometry
    • Walzthoeni, T. et al. False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nature Methods 9, 901-903 (2012).
    • (2012) Nature Methods , vol.9 , pp. 901-903
    • Walzthoeni, T.1
  • 41
    • 77949676526 scopus 로고    scopus 로고
    • A guided tour of the Trans-Proteomic Pipeline
    • Deutsch, E. W. et al. A guided tour of the Trans-Proteomic Pipeline. Proteomics 10, 1150-1159 (2010).
    • (2010) Proteomics , vol.10 , pp. 1150-1159
    • Deutsch, E.W.1
  • 42
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M. & Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 44
    • 84861178173 scopus 로고    scopus 로고
    • Platform-independent and label-free quantitation of proteomic data using MS1 extracted ion chromatograms in skyline: Application to protein acetylation and phosphorylation
    • Schilling, B. et al. Platform-independent and label-free quantitation of proteomic data using MS1 extracted ion chromatograms in skyline: application to protein acetylation and phosphorylation. Mol. Cell. Proteom. 11, 202-214 (2012).
    • (2012) Mol. Cell. Proteom. , vol.11 , pp. 202-214
    • Schilling, B.1
  • 46
    • 84907273830 scopus 로고    scopus 로고
    • Comparison of label-free quantification methods for the determination of protein complexes subunits stoichiometry
    • Fabre, B. et al. Comparison of label-free quantification methods for the determination of protein complexes subunits stoichiometry. EUPROT 4, 82-86 (2014).
    • (2014) EUPROT , vol.4 , pp. 82-86
    • Fabre, B.1
  • 47
    • 16644377031 scopus 로고    scopus 로고
    • Interactive electron-density map interpretation: From INTER to O
    • Jones, T. A. Interactive electron-density map interpretation: from INTER to O. Acta Crystallogr. D 60, 2115-2125 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2115-2125
    • Jones, T.A.1
  • 48
    • 84889120137 scopus 로고
    • Improved methods for building proteinmodels in electron densitymaps and the location of errors in thesemodels
    • Jones, T. A., Zou, J. Y., Cowan,S. W.&Kjeldgaard, M.Improved methods for building proteinmodels in electron densitymaps and the location of errors in thesemodels. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 50
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A. & Sternberg, M. J. E. Protein structure prediction on the Web: a case study using the Phyre server. Nature Protocols 4, 363-371 (2009).
    • (2009) Nature Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 51
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 52
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149 (1986).
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 53
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 333, 721-745 (2003).
    • (2003) J.Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 54
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 56
    • 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
  • 57
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.