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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


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Disease relevance of Ribosomes


Psychiatry related information on Ribosomes

  • Dendritic localization, which was confirmed by co-fractionation of FMRP with synaptosomal ribosomes, suggests a possible role of FMRP in the translation of proteins involved in dendritic structure or function and relevant for the mental retardation occurring in fragile X syndrome [6].
  • There is clearly a burst of ribosome synthesis starting as early as 30 min after copulation and declining after 6 h [7].

High impact information on Ribosomes

  • Part of the additional binding energy of cognate tRNA is used to induce conformational changes in the ribosome that stabilize a transition state for GTP hydrolysis by EF-Tu and subsequently result in accelerated accommodation of tRNA into the peptidyl transferase center [8].
  • The ribosome discriminates between correct and incorrect aminoacyl-tRNAs (aa-tRNAs), or their complexes with elongation factor Tu (EF-Tu) and GTP, according to the match between anticodon and mRNA codon in the A site [9].
  • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation [10].
  • Eukaryotic translation initiation factor 4F (eIF4F) is a protein complex that mediates recruitment of ribosomes to mRNA [10].
  • Unique tRNAs that have complementary UCA anticodons are aminoacylated with serine, the seryl-tRNA is converted to selenocysteyl-tRNA and the latter binds specifically to a special elongation factor and is delivered to the ribosome [11].

Chemical compound and disease context of Ribosomes


Biological context of Ribosomes


Anatomical context of Ribosomes

  • Unspliced HAC1 mRNA is stable, located in the cytosol, and is associated with polyribosomes, yet does not produce protein, indicating that the ribosomes engaged on the mRNA are stalled [22].
  • The mRNA for the viral glycoprotein (G), known to translate only on ribosomes bound to endoplasmic reticulum, is also retained by the detergent-extracted structure [23].
  • Binding of bromouridine-substituted reovirus mRNA to ribosomes was inhibited to the greatest extent, while binding of inosine-substituted reovirus mRNA was not inhibited at all in the reticulocyte lysate system or was slightly inhibited in a wheat-germ system [24].
  • The division of labor between RNA and protein illustrated by this simple system reveals principles applicable to complex ribonucleoprotein assemblies such as the spliceosome and ribosome [25].
  • Explanations have included the use by mitochondria of codons requiring a specialized tRNA population and the fortuitous occurrence within genes of purine-rich sequences resembling bacterial ribosome binding sites [26].

Associations of Ribosomes with chemical compounds

  • While pre-steady-state kinetic analysis of the peptidyl transferase activity of the mutant ribosomes reveals substantially reduced rates of peptide bond formation using the minimal substrate puromycin, their rates of peptide bond formation are unaffected when the substrates are intact aminoacyl-tRNAs [27].
  • The isolation of a class of partial revertants to temperature insensitivity which have simultaneously become sensitive to streptomycin suggests that the translational requirement for the anticodon modification can be partially overcome by a change in the structure of the ribosome [28].
  • We propose that reduced elongation rates in the presence of cycloheximide allow otherwise insufficient SRP to interact efficiently with ribosomes [29].
  • Questioning of reported evidence for guanosine tetraphosphate synthesis in a ribosome system from mouse embryos [30].
  • The adaptive response to nutritional stress involves increased translation of the arginine/lysine transporter (cat-1) mRNA via an internal ribosome entry site (IRES) within the mRNA leader [31].

Gene context of Ribosomes

  • Constructions were characterized that allow ribosomes to stop selectively before, within or downstream from the galK initiation signal [32].
  • A yeast gene homologous to bacterial RNase III (RNT1) encodes a double-strand-specific endoribonuclease essential for ribosome synthesis [33].
  • We show that the polysomal, cytoplasmic pool of HAC1 mRNA is a substrate for splicing, suggesting that the stalled ribosomes may resume translation after the intron is removed [22].
  • Our interpretation is that this short sequence represents a common signal that must be recognized by the box7-encoded mRNA maturase, in conjunction with the mitochondrial ribosome, to splice out the introns in the two nonhomologous genes, cob-box and oxi3 [34].
  • The FMR1 gene encodes an RNA-binding protein that associates with translating ribosomes and acts as a negative translational regulator [35].

Analytical, diagnostic and therapeutic context of Ribosomes


  1. 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. Cell (2005) [Pubmed]
  2. Mechanism of ribosome frameshifting during translation of the genetic code. Weiss, R., Gallant, J. Nature (1983) [Pubmed]
  3. Radioimmunoassay for antibodies to cytoplasmic ribosomes in human serum. Koffler, D., Faiferman, I., Gerber, M.A. Science (1977) [Pubmed]
  4. Translation by ribosome shunting on adenovirus and hsp70 mRNAs facilitated by complementarity to 18S rRNA. Yueh, A., Schneider, R.J. Genes Dev. (2000) [Pubmed]
  5. Evidence that an IRES within the Notch2 coding region can direct expression of a nuclear form of the protein. Lauring, A.S., Overbaugh, J. Mol. Cell (2000) [Pubmed]
  6. Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. Feng, Y., Gutekunst, C.A., Eberhart, D.E., Yi, H., Warren, S.T., Hersch, S.M. J. Neurosci. (1997) [Pubmed]
  7. The induction of ribosome biosynthesis in a nonmitotic secretory tissue. Schmidt, T., Chen, P.S., Pellegrini, M. J. Biol. Chem. (1985) [Pubmed]
  8. Structural insights into translational fidelity. Ogle, J.M., Ramakrishnan, V. Annu. Rev. Biochem. (2005) [Pubmed]
  9. Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms. Rodnina, M.V., Wintermeyer, W. Annu. Rev. Biochem. (2001) [Pubmed]
  10. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Gingras, A.C., Raught, B., Sonenberg, N. Annu. Rev. Biochem. (1999) [Pubmed]
  11. Selenocysteine. Stadtman, T.C. Annu. Rev. Biochem. (1996) [Pubmed]
  12. Unusual resistance of peptidyl transferase to protein extraction procedures. Noller, H.F., Hoffarth, V., Zimniak, L. Science (1992) [Pubmed]
  13. E. coli ribosomes with a C912 to U base change in the 16S rRNA are streptomycin resistant. Montandon, P.E., Wagner, R., Stutz, E. EMBO J. (1986) [Pubmed]
  14. Basis for prokaryotic specificity of action of aminoglycoside antibiotics. Recht, M.I., Douthwaite, S., Puglisi, J.D. EMBO J. (1999) [Pubmed]
  15. Arginines 29 and 59 of elongation factor G are important for GTP hydrolysis or translocation on the ribosome. Mohr, D., Wintermeyer, W., Rodnina, M.V. EMBO J. (2000) [Pubmed]
  16. Nascent peptide as sole attachment of polysomes to membranes in bacteria. Smith, W.P., Tai, P.C., Davis, B.D. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  17. Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function. Atkins, J.F., Steitz, J.A., Anderson, C.W., Model, P. Cell (1979) [Pubmed]
  18. Exploration of essential gene functions via titratable promoter alleles. Mnaimneh, S., Davierwala, A.P., Haynes, J., Moffat, J., Peng, W.T., Zhang, W., Yang, X., Pootoolal, J., Chua, G., Lopez, A., Trochesset, M., Morse, D., Krogan, N.J., Hiley, S.L., Li, Z., Morris, Q., Grigull, J., Mitsakakis, N., Roberts, C.J., Greenblatt, J.F., Boone, C., Kaiser, C.A., Andrews, B.J., Hughes, T.R. Cell (2004) [Pubmed]
  19. Regulation of ribosome phosphorylation and antibiotic sensitivity in Tetrahymena thermophila: A correlation. Hallberg, R.L., Wilson, P.G., Sutton, C. Cell (1981) [Pubmed]
  20. Coupling of GCN4 mRNA translational activation with decreased rates of polypeptide chain initiation. Tzamarias, D., Roussou, I., Thireos, G. Cell (1989) [Pubmed]
  21. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Shin, B.S., Maag, D., Roll-Mecak, A., Arefin, M.S., Burley, S.K., Lorsch, J.R., Dever, T.E. Cell (2002) [Pubmed]
  22. Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Rüegsegger, U., Leber, J.H., Walter, P. Cell (2001) [Pubmed]
  23. Messenger RNA is translated when associated with the cytoskeletal framework in normal and VSV-infected HeLa cells. Cervera, M., Dreyfuss, G., Penman, S. Cell (1981) [Pubmed]
  24. Probing the function of the eucaryotic 5' cap structure by using a monoclonal antibody directed against cap-binding proteins. Sonenberg, N., Guertin, D., Cleveland, D., Trachsel, H. Cell (1981) [Pubmed]
  25. Protein facilitation of group I intron splicing by assembly of the catalytic core and the 5' splice site domain. Weeks, K.M., Cech, T.R. Cell (1995) [Pubmed]
  26. In vitro suppression of UGA codons in a mitochondrial mRNA. De Ronde, A., Van Loon, A.P., Grivell, L.A., Kohli, J. Nature (1980) [Pubmed]
  27. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Youngman, E.M., Brunelle, J.L., Kochaniak, A.B., Green, R. Cell (2004) [Pubmed]
  28. A functional requirement for modification of the wobble nucleotide in tha anticodon of a T4 suppressor tRNA. Colby, D.S., Schedl, P., Guthrie, C. Cell (1976) [Pubmed]
  29. SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Ogg, S.C., Walter, P. Cell (1995) [Pubmed]
  30. Questioning of reported evidence for guanosine tetraphosphate synthesis in a ribosome system from mouse embryos. Martini, O., Irr, J., Richter, D. Cell (1977) [Pubmed]
  31. The zipper model of translational control: a small upstream ORF is the switch that controls structural remodeling of an mRNA leader. Yaman, I., Fernandez, J., Liu, H., Caprara, M., Komar, A.A., Koromilas, A.E., Zhou, L., Snider, M.D., Scheuner, D., Kaufman, R.J., Hatzoglou, M. Cell (2003) [Pubmed]
  32. Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon. Schümperli, D., McKenney, K., Sobieski, D.A., Rosenberg, M. Cell (1982) [Pubmed]
  33. RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site. Elela, S.A., Igel, H., Ares, M. Cell (1996) [Pubmed]
  34. Critical sequences within mitochondrial introns: cis-dominant mutations of the "cytochrome-b-like" intron of the oxidase gene. Netter, P., Jacq, C., Carignani, G., Slonimski, P.P. Cell (1982) [Pubmed]
  35. A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins. Ishizuka, A., Siomi, M.C., Siomi, H. Genes Dev. (2002) [Pubmed]
  36. The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking. McCallum, C.D., Do, H., Johnson, A.E., Frydman, J. J. Cell Biol. (2000) [Pubmed]
  37. Recovery of ribophorins and ribosomes in "inverted rough" vesicles derived from rat liver rough microsomes. Kreibich, G., Ojakian, G., Rodriguez-Boulan, E., Sabatini, D.D. J. Cell Biol. (1982) [Pubmed]
  38. Nascent polypeptide chains exit the ribosome in the same relative position in both eucaryotes and procaryotes. Bernabeu, C., Tobin, E.M., Fowler, A., Zabin, I., Lake, J.A. J. Cell Biol. (1983) [Pubmed]
  39. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Agrawal, R.K., Heagle, A.B., Penczek, P., Grassucci, R.A., Frank, J. Nat. Struct. Biol. (1999) [Pubmed]
  40. Restoration of blood flow by using continuous perimuscular infiltration of plasmid DNA encoding subterranean mole rat Spalax ehrenbergi VEGF. Roguin, A., Avivi, A., Nitecki, S., Rubinstein, I., Levy, N.S., Abassi, Z.A., Resnick, M.B., Lache, O., Melamed-Frank, M., Joel, A., Hoffman, A., Nevo, E., Levy, A.P. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
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