Abstract
In the past decade, tremendous progress has been made in elucidating the structure and function of the ribosome (reviewed in Schmeing and Ramakrishnan, 2009). Numerous x-ray crystal structures and cryo-electron microscopic (cryo-EM) reconstructions of the ribosome with and without various substrates, factors, and antibiotics have been solved. At the same time, extensive biochemical studies have led to compelling kinetic models for the major steps of protein synthesis. While these studies give us a high-resolution picture of the ribosome and suggest a series of events involved in translation, the roles of specific ribosomal elements in particular events of the process remain unclear. Studies of mutations that confer altered function, particularly those in rRNA, will undoubtedly provide insight about these structure-function relationships.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abdi NM, Fredrick, K (2005) Contribution of 16S rRNA nucleotides forming the 30S subunit A and P sites to translation in Escherichia coli. RNA 11: 1624–1632
Allen PN, Noller HF (1991) A single base substitution in 16S ribosomal RNA suppresses streptomycin dependence and increases the frequency of translational errors. Cell 66: 141–148
Arkov AL, Freistroffer DV, Ehrenberg M, Murgola EJ (1998) Mutations in RNAs of both ribosomal subunits cause defects in translation termination. EMBO J 17: 1507–1514
Arkov AL, Freistroffer DV, Pavlov MY, Ehrenberg M, Murgola EJ (2000) Mutations in conserved regions of ribosomal RNAs decrease the productive association of peptide-chain release factors with the ribosome during translation termination. Biochimie 82: 671–682
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
Cupples CG, Miller JH (1988) Effects of amino acid substitutions at the active site in Escherichia coli beta-galactosidase. Genetics 120: 637–644
Cupples CG, Miller JH (1989) A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc Natl Acad Sci USA 86: 5345–5349
Dallas A, Noller HF (2001) Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol Cell 8: 855–864
Devaraj A, Shoji S, Holbrook ED, Fredrick, K (2009) A role for the 30S subunit E site in maintenance of the translational reading frame. RNA 15: 255–265
Feliu JX, Villaverde, A (1998) Engineering of solvent-exposed loops in Escherichia coli beta-galactosidase. FEBS Lett 434: 23–27
Fu C, Parker, J (1994) A ribosomal frameshifting error during translation of the argI mRNA of Escherichia coli. Mol Gen Genet 243: 434–441
Gregory ST, Dahlberg AE (1995) Nonsense suppressor and antisuppressor mutations at the 1409–1491 base pair in the decoding region of Escherichia coli 16S rRNA. Nucleic Acids Res 23: 4234–4238
Haggerty TJ, Lovett ST (1997) IF3-mediated suppression of a GUA initiation codon mutation in the recJ gene of Escherichia coli. J Bacteriol 179: 6705–6713
Hui A, and de Boer HA (1987) Specialized ribosome system: preferential translation of a single mRNA species by a subpopulation of mutated ribosomes in Escherichia coli. Proc Natl Acad Sci USA 84: 4762–4766
Lee K, Holland-Staley CA, Cunningham PR (1996) Genetic analysis of the Shine-Dalgarno interaction: selection of alternative functional mRNA-rRNA combinations. RNA 2: 1270–1285
Leger M, Dulude D, Steinberg SV, Brakier-Gingras, L (2007) The three transfer RNAs occupying the A, P and E sites on the ribosome are involved in viral programmed-1 ribosomal frameshift. Nucleic Acids Res 35: 5581–5592
Lodmell JS, Dahlberg AE (1997) A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA. Science 277: 1262–1267
Maisnier-Patin S, Paulander W, Pennhag A, Andersson DI (2007) Compensatory evolution reveals functional interactions between ribosomal proteins S12, L14 and L19. J Mol Biol 366: 207–215
McClory SP, Leisring JM, Qin D, Fredrick, K (2010) Missense suppressor mutations in 16S rRNA reveal the importance of helices h8 and h 14 in aminoacyl-tRNA selection. RNA 16: 1925–1934
Moine H, Dahlberg AE (1994) Mutations in helix 34 of Escherichia coli 16 S ribosomal RNA have multiple effects on ribosome function and synthesis. J Mol Biol 243: 402–412
Murgola EJ, Pagel FT, Hijazi KA, Arkov AL, Xu W, Zhao SQ (1995) Variety of nonsense suppressor phenotypes associated with mutational changes at conserved sites in Escherichia coli ribosomal RNA. Biochem Cell Biol 73: 925–931
O’ Connor M, Thomas CL, Zimmermann RA, Dahlberg AE (1997) Decoding fidelity at the ribosomal A and P sites: influence of mutations in three different regions of the decoding domain in 16S rRNA. Nucleic Acids Res 25: 1185–1193
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
Ogle JM, Ramakrishnan, V (2005) Structural insights into translational fidelity. Annu Rev Biochem 74: 129–177
Pagel FT, Zhao SQ, Hijazi KA, Murgola EJ (1997) Phenotypic heterogeneity of mutational changes at a conserved nucleotide in 16 S ribosomal RNA. J Mol Biol 267: 1113–1123
Qin D, Abdi NM, Fredrick, K (2007) Characterization of 16S rRNA mutations that decrease the fidelity of translation initiation. RNA 13: 2348–2355
Qin D, Fredrick, K (2009) Control of translation initiation involves a factor-induced rearrangement of helix 44 of 16S ribosomal RNA. Mol Microbiol 71: 1239–1249
Rosset R, Gorini, L (1969) A ribosomal ambiguity mutation. J Mol Biol 39: 95–112
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 FV 4th, Weir JR, Ramakrishnan, V (2009) The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326: 688–694
Selmer M, Dunham CM, Murphy FV 4th, 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
Strigini P, Gorini, L (1970) Ribosomal mutations affecting efficiency of amber suppression. J Mol Biol 47: 517–530
Sussman JK, Simons EL, Simons RW (1996) Escherichia coli translation initiation factor 3 discriminates the initiation codon in vivo. Mol Microbiol 21: 347–360
Tapprich WE, Goss DJ, Dahlberg AE (1989) Mutation at position 791 in Escherichia coli 16S ribosomal RNA affects processes involved in the initiation of protein synthesis. Proc Natl Acad Sci USA 86: 4927–4931
Velichutina IV, Dresios J, Hong JY, Li C, Mankin A, Synetos D, Liebman SW (2000) Mutations in helix 27 of the yeast Saccharomyces cerevisiae 18S rRNA affect the function of the decoding center of the ribosome. RNA 6: 1174–1184
Villa E, Sengupta J, Trabuco LG, LeBarron J, Baxter WT, Shaikh TR, Grassucci RA, Nissen P, Ehrenberg M, Schulten K, Frank, J (2009) Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc Natl Acad Sci USA 106: 1063–1068
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 A, Fredrick K, Mankin AS (2005) Deleterious mutations in small subunit ribosomal RNA identify functional sites and potential targets for antibiotics. Proc Natl Acad Sci USA 102: 16620–16625
Zhang W, Dunkle JA, Cate JH (2009) Structures of the ribosome in intermediate states of ratcheting. Science 325: 1014–1017
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer-Verlag/Wien
About this chapter
Cite this chapter
McClory, S.P., Devaraj, A., Qin, D., Leisring, J.M., Fredrick, K. (2011). Mutations in 16S rRNA that decrease the fidelity of translation. In: Rodnina, M.V., Wintermeyer, W., Green, R. (eds) Ribosomes. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0215-2_19
Download citation
DOI: https://doi.org/10.1007/978-3-7091-0215-2_19
Publisher Name: Springer, Vienna
Print ISBN: 978-3-7091-0214-5
Online ISBN: 978-3-7091-0215-2
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)