Abstract
Mitochondrial ribosomes are known to be quite divergent from cytoplasmic ribosomes in both composition and structure even as their main functional cores, such as the mRNA decoding and peptidyl transferase sites, are highly conserved. The translational factors that interact with these ribosomes to facilitate the process of protein synthesis in mitochondria have also likewise acquired unique structural features, apparently to complement the structure and function of the mitochondrial ribosome. In this chapter, we describe the current state of structural knowledge of the mammalian mitochondrial ribosome, some of its component proteins, and key translational factors.
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References
Ӕvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A (1994) Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J 13:3669–3677
Agirrezabala X, Frank J (2009) Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu. Q Rev Biophys 42:159–200
Agirrezabala X, Schreiner E, Trabuco LG, Lei J, Ortiz-Meoz RF, Schulten K, Green R, Frank J (2011) Structural insights into cognate versus near-cognate discrimination during decoding. EMBO J 30:1497–1507
Agrawal RK, Sharma MR (2012) Structural aspects of mitochondrial translational apparatus. Curr Opin Struct Biol 22:797–803
Agrawal RK, Penczek P, Grassucci RA, Frank J (1998) Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. Proc Natl Acad Sci U S A 95:6134–6138
Agrawal RK, Heagle AB, Penczek P, Grassucci RA, Frank J (1999) EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat Struct Biol 6:643–647
Agrawal RK, Spahn CM, Penczek P, Grassucci RA, Nierhaus KH, Frank J (2000) Visualization of tRNA movements on the Escherichia coli 70S ribosome during the elongation cycle. J Cell Biol 150:447–460
Agrawal RK, Sharma MR, Kiel MC, Hirokawa G, Booth TM, Spahn CM, Grassucci RA, Kaji A, Frank J (2004) Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications. Proc Natl Acad Sci U S A 101:8900–8905
Agrawal RK, Sharma MR, Yassin AS, Lahiri I, Spremulli L (2011) Structure and function of organellar ribosomes as revealed by cryo-EM. In: Rodnina M, Wintermeyer W, Green R (eds) Ribosomes: structure, function, and dynamics. SpringerWien, New York, pp 83–96
Akama K, Christian BE, Jones CN, Ueda T, Takeuchi N, Spremulli LL (2010) Analysis of the functional consequences of lethal mutations in mitochondrial translational elongation factors. Biochim Biophys Acta 1802:692–698
Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J (2005) The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121:703–712
Antonicka H, Ostergaard E, Sasarman F, Weraarpachai W, Wibrand F, Pedersen AM, Rodenburg RJ, van der Knaap MS, Smeitink JA, Chrzanowska-Lightowlers ZM et al (2010) Mutations in C12orf65 in patients with encephalomyopathy and a mitochondrial translation defect. Am J Hum Genet 87:115–122
Atkinson GC, Baldauf SL (2011) Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms. Mol Biol Evol 28:1281–1292
Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289:905–920
Barat C, Datta PP, Raj VS, Sharma MR, Kaji H, Kaji A, Agrawal RK (2007) Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits. Mol Cell 27:250–261
Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M (2011) The structure of the eukaryotic ribosome at 3.0 Å resolution. Science 334:1524–1529
Bhargava K, Spremulli LL (2005) Role of the N- and C-terminal extensions on the activity of mammalian mitochondrial translational initiation factor 3. Nucleic Acids Res 33:7011–7018
Bhargava K, Templeton P, Spremulli LL (2004) Expression and characterization of isoform 1 of human mitochondrial elongation factor G. Protein Expr Purif 37:368–376
Biou V, Shu F, Ramakrishnan V (1995) X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. EMBO J 14:4056–4064
Bullard JM, Cai YC, Zhang Y, Spremulli LL (1999) Effects of domain exchanges between Escherichia coli and mammalian mitochondrial EF-Tu on interactions with guanine nucleotides, aminoacyl-tRNA and ribosomes. Biochim Biophys Acta 1446:102–114
Carter AP, Clemons WM Jr, Brodersen DE, Morgan-Warren RJ, Hartsch T, Wimberly BT, Ramakrishnan V (2001) Crystal structure of an initiation factor bound to the 30S ribosomal subunit. Science 291:498–501
Christian BE, Spremulli LL (2009) Evidence for an active role of IF3mt in the initiation of translation in mammalian mitochondria. Biochemistry 48:3269–3278
Christian BE, Spremulli LL (2010) Preferential selection of the 5′-terminal start codon on leaderless mRNAs by mammalian mitochondrial ribosomes. J Biol Chem 285:28379–28386
Christian BE, Spremulli LL (2012) Mechanism of protein biosynthesis in mammalian mitochondria. Biochim Biophys Acta 1819:1035–1054
Chrzanowska-Lightowlers ZM, Pajak A, Lightowlers RN (2011) Termination of protein synthesis in mammalian mitochondria. J Biol Chem 286:34479–34485
Chung HK, Spremulli LL (1990) Purification and characterization of elongation factor G from bovine liver mitochondria. J Biol Chem 265:21000–21004
Claros MG, Vincens P (1996) Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241:779–786
Czworkowski J, Wang J, Steitz TA, Moore PB (1994) The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J 13:3661–3668
Dallas A, Noller HF (2001) Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol Cell 8:855–864
Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK (2005) Interaction of the G’ domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM. Mol Cell 20:723–731
Duarte I, Nabuurs SB, Magno R, Huynen M (2012) Evolution and diversification of the organellar release factor family. Mol Biol Evol 29:3497–3512
Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH (2011) Structures of the bacterial ribosome in classical and hybrid states of tRNA binding. Science 332:981–984
Frank J, Agrawal RK (2000) A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 406:318–322
Frank J, Agrawal RK (2001) Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation. Cold Spring Harb Symp Quant Biol 66:67–75
Frank J, Penczek P, Agrawal RK, Grassucci RA, Heagle AB (2000) Three-dimensional cryoelectron microscopy of ribosomes. Methods Enzymol 317:276–291
Gabashvili IS, Agrawal RK, Spahn CM, Grassucci R, Svergun D, Frank J, Penczek P (2000) Solution structure of the E. coli 70S ribosome at 11.5 Å resolution. Cell 100:537–549
Gagnon MG, Seetharaman SV, Bulkley D, Steitz TA (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science 335:1370–1372
Gao N, Zavialov AV, Li W, Sengupta J, Valle M, Gursky RP, Ehrenberg M, Frank J (2005) Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies. Mol Cell 18:663–674
Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V (2009) The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326:694–699
Gaur R, Grasso D, Datta PP, Krishna PD, Das G, Spencer A, Agrawal RK, Spremulli L, Varshney U (2008) A single mammalian mitochondrial translation initiation factor functionally replaces two bacterial factors. Mol Cell 29:180–190
Gomez-Lorenzo MG, Spahn CM, Agrawal RK, Grassucci RA, Penczek P, Chakraburtty K, Ballesta JP, Lavandera JL, Garcia-Bustos JF, Frank J (2000) Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 A resolution. EMBO J 19:2710–2718
Gray, M.W., Burger, G., and Lang, B.F. (2001). The origin and early evolution of mitochondria. Genome Biol 2, REVIEWS1018
Gruschke S, Ott M (2010) The polypeptide tunnel exit of the mitochondrial ribosome is tailored to meet the specific requirements of the organelle. BioEssays 32:1050–1057
Hammarsund M, Wilson W, Corcoran M, Merup M, Einhorn S, Grander D, Sangfelt O (2001) Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution. Hum Genet 109:542–550
Hanada T, Suzuki T, Watanabe K (2000) Translation activity of mitochondrial tRNA with unusual secondary structure. Nucleic Acids Symp Ser 44:249–250
Haque ME, Spremulli LL (2008) Roles of the N- and C-terminal domains of mammalian mitochondrial initiation factor 3 in protein biosynthesis. J Mol Biol 384:929–940
Haque ME, Spremulli LL, Fecko CJ (2010) Identification of protein–protein and protein-ribosome interacting regions of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L. J Biol Chem 285:34991–34998
Haque ME, Koc H, Cimen H, Koc EC, Spremulli LL (2011) Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit. Biochim Biophys Acta 1814:1779–1784
Huynen MA, Duarte I, Chrzanowska-Lightowlers ZM, Nabuurs SB (2012) Structure based hypothesis of a mitochondrial ribosome rescue mechanism. Biol Direct 7:14
Jeppesen MG, Navratil T, Spremulli LL, Nyborg J (2005) Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex. J Biol Chem 280:5071–5081
Jia L, Dienhart M, Schramp M, McCauley M, Hell K, Stuart RA (2003) Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1. EMBO J 22:6438–6447
Julian P, Milon P, Agirrezabala X, Lasso G, Gil D, Rodnina MV, Valle M (2011) The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS Biol 9:e1001095
Keil M, Bareth B, Woellhaf MW, Peleh V, Prestele M, Rehling P, Herrmann JM (2012) Oxa1-ribosome complexes coordinate the assembly of cytochrome C oxidase in mitochondria. J Biol Chem 287:34484–34493
Kjeldgaard M, Nissen P, Thirup S, Nyborg J (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1:35–50
Klinge S, Voigts-Hoffmann F, Leibundgut M, Arpagaus S, Ban N (2011) Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6. Science 334:941–948
Koc EC, Koc H (2012) Regulation of mammalian mitochondrial translation by post-translational modifications. Biochim Biophys Acta 1819:1055–1066
Koc EC, Burkhart W, Blackburn K, Moseley A, Koc H, Spremulli LL (2000) A proteomics approach to the identification of mammalian mitochondrial small subunit ribosomal proteins. J Biol Chem 275:32585–32591
Koc EC, Burkhart W, Blackburn K, Moseley A, Spremulli LL (2001a) The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. J Biol Chem 276:19363–19374
Koc EC, Burkhart W, Blackburn K, Moyer MB, Schlatzer DM, Moseley A, Spremulli LL (2001b) The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present. J Biol Chem 276:43958–43969
Koc EC, Haque ME, Spremulli LL (2010) Current views of the structure of the mammalian mitochondrial ribosome. Isr J Chem 50:45–59
Korostelev AA (2011) Structural aspects of translation termination on the ribosome. RNA 17:1409–1421
Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF (2008) Structural basis for translation termination on the 70S ribosome. Nature 454:852–857
Luirink J, Samuelsson T, de Gier JW (2001) YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly. FEBS Lett 501:1–5
Manuell AL, Quispe J, Mayfield SP (2007) Structure of the chloroplast ribosome: novel domains for translation regulation. PLoS Biol 5:e209
McCutcheon JP, Agrawal RK, Philips SM, Grassucci RA, Gerchman SE, Clemons WM Jr, Ramakrishnan V, Frank J (1999) Location of translational initiation factor IF3 on the small ribosomal subunit. Proc Natl Acad Sci U S A 96:4301–4306
Mears JA, Sharma MR, Gutell RR, McCook AS, Richardson PE, Caulfield TR, Agrawal RK, Harvey SC (2006) A structural model for the large subunit of the mammalian mitochondrial ribosome. J Mol Biol 358:193–212
Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J (1995) Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 270:1464–1472
Nissen P, Hansen J, Ban N, Moore PB, Steitz TA (2000) The structural basis of ribosome activity in peptide bond synthesis. Science 289:920–930
O’Brien TW (2002) Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease. Gene 286:73–79
O’Brien TW, O’Brien BJ, Norman RA (2005) Nuclear MRP genes and mitochondrial diseases. Gene 354:147–151
Ogle JM, Brodersen DE, Clemons WM Jr, Tarry MJ, Carter AP, Ramakrishnan V (2001) Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292:897–902
Ohtsuki T, Watanabe Y (2007) T-armless tRNAs and elongated elongation factor Tu. IUBMB Life 59:68–75
Ott M, Herrmann JM (2010) Co-translational membrane insertion of mitochondrially encoded proteins. Biochim Biophys Acta 1803:767–775
Pai RD, Zhang W, Schuwirth BS, Hirokawa G, Kaji H, Kaji A, Cate JH (2008) Structural Insights into ribosome recycling factor interactions with the 70S ribosome. J Mol Biol 376:1334–1347
Pearce S, Nezich CL, Spinazzola A (2013) Mitochondrial diseases: translation matters. Mol Cell Neurosci 55:1–12
Petrelli D, LaTeana A, Garofalo C, Spurio R, Pon CL, Gualerzi CO (2001) Translation initiation factor IF3: two domains, five functions, one mechanism? EMBO J 20:4560–4569
Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (2004) UCSF Chimera–a visualization system for exploratory research and analysis. J Comput Chem 25:1605–1612
Rawat UB, Zavialov AV, Sengupta J, Valle M, Grassucci RA, Linde J, Vestergaard B, Ehrenberg M, Frank J (2003) A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421:87–90
Richter R, Rorbach J, Pajak A, Smith PM, Wessels HJ, Huynen MA, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZM (2010) A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome. EMBO J 29:1116–1125
Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kuhl I, Gaisne M, Bonnefoy N, Smeitink JA et al (2008) The human mitochondrial ribosome recycling factor is essential for cell viability. Nucleic Acids Res 36:5787–5799
Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5:725–738
Schmeing TM, Ramakrishnan V (2009) What recent ribosome structures have revealed about the mechanism of translation. Nature 461:1234–1242
Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FVt, Weir JR JR, Ramakrishnan V (2009) The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326:688–694
Schuette JC, Murphy FVt, Kelley AC, Weir JR, Giesebrecht J, Connell SR, Loerke J, Mielke T, Zhang W, Penczek PA et al (2009) GTPase activation of elongation factor EF-Tu by the ribosome during decoding. EMBO J 28:755–765
Schuwirth BS, Borovinskaya MA, Hau CW, Zhang W, Vila-Sanjurjo A, Holton JM, Cate JH (2005) Structures of the bacterial ribosome at 3.5 Å resolution. Science 310:827–834
Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A (1999) Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science 286:2349–2352
Selmer M, Dunham CM, Murphy FVt, Weixlbaumer A, Petry S, Kelley AC, Weir JR, Ramakrishnan V (2006) Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313:1935–1942
Sharma MR, Koc EC, Datta PP, Booth TM, Spremulli LL, Agrawal RK (2003) Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115:97–108
Sharma MR, Wilson DN, Datta PP, Barat C, Schluenzen F, Fucini P, Agrawal RK (2007) Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins. Proc Natl Acad Sci U S A 104:19315–19320
Sharma MR, Booth TM, Simpson L, Maslov DA, Agrawal RK (2009) Structure of a mitochondrial ribosome with minimal RNA. Proc Natl Acad Sci U S A 106:9637–9642
Sharma MR, Dönhöfer A, Barat C, Marquez V, Datta PP, Fucini P, Wilson DN, Agrawal RK (2010) PSRP1 is not a ribosomal protein, but a ribosome-binding factor that is recycled by the ribosome-recycling factor (RRF) and elongation factor G (EF-G). J Biol Chem 285:4006–4014
Smirnov A, Entelis N, Martin RP, Tarassov I (2011) Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18. Genes Dev 25:1289–1305
Smits P, Smeitink JA, van den Heuvel LP, Huynen MA, Ettema TJ (2007) Reconstructing the evolution of the mitochondrial ribosomal proteome. Nucleic Acids Res 35:4686–4703
Soleimanpour-Lichaei HR, Kuhl I, Gaisne M, Passos JF, Wydro M, Rorbach J, Temperley R, Bonnefoy N, Tate W, Lightowlers R et al (2007) mtRF1a is a human mitochondrial translation release factor decoding the major termination codons UAA and UAG. Mol Cell 27:745–757
Spahn CM, Gomez-Lorenzo MG, Grassucci RA, Jorgensen R, Andersen GR, Beckmann R, Penczek PA, Ballesta JP, Frank J (2004) Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J 23:1008–1019
Spencer AC, Spremulli LL (2004) Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA. Nucleic Acids Res 32:5464–5470
Spencer AC, Spremulli LL (2005) The interaction of mitochondrial translational initiation factor 2 with the small ribosomal subunit. Biochim Biophys Acta 1750:69–81
Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel M (1997) Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature 389:403–406
Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K (2001a) Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28S small subunit. J Biol Chem 276:33181–33195
Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K (2001b) Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria. J Biol Chem 276:21724–21736
Szyrach G, Ott M, Bonnefoy N, Neupert W, Herrmann JM (2003) Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria. EMBO J 22:6448–6457
Temperley RJ, Wydro M, Lightowlers RN, Chrzanowska-Lightowlers ZM (2010) Human mitochondrial mRNAs-like members of all families, similar but different. Biochim Biophys Acta 1797:1081–1085
Tsuboi M, Morita H, Nozaki Y, Akama K, Ueda T, Ito K, Nierhaus KH, Takeuchi N (2009) EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell 35:502–510
Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J (2002) Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J 21:3557–3567
Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M (2001) Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 8:1375–1382
Watanabe K (2010) Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus and their relevance to human mitochondrial diseases. Proc Jpn Acad Ser B Phys Biol Sci 86:11–39
Weixlbaumer A, Petry S, Dunham CM, Selmer M, Kelley AC, Ramakrishnan V (2007) Crystal structure of the ribosome recycling factor bound to the ribosome. Nat Struct Mol Biol 14:733–737
Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V (2008) Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322:953–956
Wimberly BT, Brodersen DE, Clemons WM Jr, Morgan-Warren RJ, Carter AP, Vonrhein C, Hartsch T, Ramakrishnan V (2000) Structure of the 30S ribosomal subunit. Nature 407:327–339
Yassin AS, Agrawal RK, Banavali NK (2011a) Computational exploration of structural hypotheses for an additional sequence in a mammalian mitochondrial protein. PLoS ONE 6:e21871
Yassin AS, Haque ME, Datta PP, Elmore K, Banavali NK, Spremulli LL, Agrawal RK (2011b) Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1. Proc Natl Acad Sci U S A 108:3918–3923
Yokoyama T, Shaikh TR, Iwakura N, Kaji H, Kaji A, Agrawal RK (2012) Structural insights into initial and intermediate steps of the ribosome-recycling process. EMBO J 31:1836–1846
Yusupov MM, Yusupova GZ, Baucom A, Lieberman K, Earnest TN, Cate JH, Noller HF (2001) Crystal structure of the ribosome at 5.5 Å resolution. Science 292:883–896
Yusupova GZ, Yusupov MM, Cate JH, Noller HF (2001) The path of messenger RNA through the ribosome. Cell 106:233–241
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This work was supported by the National Institutes of Health grant R01 GM61576 (to R.K.A.).
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Sharma, M.R., Kaushal, P.S., Gupta, M., Banavali, N.K., Agrawal, R.K. (2013). Insights into Structural Basis of Mammalian Mitochondrial Translation. In: Duchêne, AM. (eds) Translation in Mitochondria and Other Organelles. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-39426-3_1
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