peptide termination factors

Summary

Summary: Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.

Top Publications

  1. Wickner R, Shewmaker F, Kryndushkin D, Edskes H. Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures. Bioessays. 2008;30:955-64 pubmed publisher
    ..This property of self-reproduction, in turn, allows these proteins to act as de facto genes, encoding heritable information. ..
  2. Young D, Edgar C, Murphy J, Fredebohm J, Poole E, Tate W. Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria. RNA. 2010;16:1146-55 pubmed publisher
    ..These observations imply that MTRF1 has the characteristics to recognize A as the first base of a stop codon as would be required to decode the nonstandard codons AGA and AGG. ..
  3. Tyedmers J, Treusch S, Dong J, McCaffery J, Bevis B, Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci U S A. 2010;107:8633-8 pubmed publisher
    ..Thus, formation of the genetically transmissible prion state is a two-step process that involves an ancient system for the asymmetric inheritance of damaged proteins and heritable changes in the extent of prion fragmentation. ..
  4. Krammer C, Suhre M, Kremmer E, Diemer C, Hess S, Schatzl H, et al. Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells. FASEB J. 2008;22:762-73 pubmed
  5. Tuite M, Cox B. The genetic control of the formation and propagation of the [PSI+] prion of yeast. Prion. 2007;1:101-9 pubmed
    ..In this Chapter we describe what has emerged from the application of classical and molecular genetic studies, to the most intensively studied of the three native yeast prions, the [PSI(+)] prion. ..
  6. Vishveshwara N, Bradley M, Liebman S. Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol. 2009;73:1101-14 pubmed publisher
    ..This suggests [PSI(+)] toxicity caused by excess Sup35p verses Sup35NMp is, respectively, through sequestration/inactivation of Sup45p verses Sup35p. ..
  7. Jiang L, Olesen I, Andersen T, Fang W, Jespersen L. Survival of Listeria monocytogenes in simulated gastrointestinal system and transcriptional profiling of stress- and adhesion-related genes. Foodborne Pathog Dis. 2010;7:267-74 pubmed publisher
    ..Taken together, this study revealed that L. monocytogenes strains enhanced the expression of stress-related genes and decreased the transcription of adhesion-related gene in order to survive in the diverse microenvironments. ..
  8. Mantsyzov A, Ivanova E, Birdsall B, Alkalaeva E, Kryuchkova P, Kelly G, et al. NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor. FEBS J. 2010;277:2611-27 pubmed publisher
    ..Mutations in the tip of the minidomain were found to affect the stop codon specificity of the factor. The results provide new insights into the possible role of the C-domain in the process of translation termination. ..
  9. McGann P, Wiedmann M, Boor K. The alternative sigma factor sigma B and the virulence gene regulator PrfA both regulate transcription of Listeria monocytogenes internalins. Appl Environ Microbiol. 2007;73:2919-30 pubmed
    ..Interplay between sigma(B) and PrfA also appears to be critical for regulating transcription of some virulence genes, including inlA, inlB, and prfA. ..

More Information

Publications103 found, 100 shown here

  1. von der Haar T, Jossé L, Wright P, Zenthon J, Tuite M. Development of a novel yeast cell-based system for studying the aggregation of Alzheimer's disease-associated Abeta peptides in vivo. Neurodegener Dis. 2007;4:136-47 pubmed
    ..We conclude that we have established a useful new tool for studying the aggregation of Abeta peptides in an organism in vivo. ..
  2. Akhmaloka -, Susilowati P, Subandi -, Madayanti F. Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3. Int J Biol Sci. 2008;4:87-95 pubmed
    ..The data suggested that increasing stop codon suppression and decreasing of the binding affinity of eRF1(Y410S) were probably due to the slight modification on the structure of the C-terminal domain. ..
  3. Wickner R, Shewmaker F, Edskes H, Kryndushkin D, Nemecek J, McGlinchey R, et al. Prion amyloid structure explains templating: how proteins can be genes. FEMS Yeast Res. 2010;10:980-91 pubmed publisher
    ..The prion domain sequences generally vary more rapidly in evolution than does the remainder of the molecule, producing a barrier to prion transmission, perhaps selected in evolution by this protection. ..
  4. Mora L, Heurgué Hamard V, de Zamaroczy M, Kervestin S, Buckingham R. Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo. J Biol Chem. 2007;282:35638-45 pubmed
    ..This suggests that the expression of some genes needed for optimal growth under such conditions can become growth limiting as a result of inefficient translation termination. ..
  5. Fabret C, Cosnier B, Lekomtsev S, Gillet S, Hatin I, Le Marechal P, et al. A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability. BMC Mol Biol. 2008;9:22 pubmed publisher
    ..They also raise interesting questions about the relation between GTPase activity of Sup35 and its essential function in yeast. ..
  6. Kononenko A, Mitkevich V, Atkinson G, Tenson T, Dubovaya V, Frolova L, et al. GTP-dependent structural rearrangement of the eRF1:eRF3 complex and eRF3 sequence motifs essential for PABP binding. Nucleic Acids Res. 2010;38:548-58 pubmed publisher
    ..Through point mutagenesis of PAM2-1 and PAM2-2 motifs in eRF3, we demonstrate that PAM2-2, but not PAM2-1 is indispensible for eRF3:PABP complex formation. ..
  7. Pisarev A, Skabkin M, Pisareva V, Skabkina O, Rakotondrafara A, Hentze M, et al. The role of ABCE1 in eukaryotic posttermination ribosomal recycling. Mol Cell. 2010;37:196-210 pubmed publisher
    ..Importantly, ABCE1 dissociates only post-TCs obtained with eRF1/eRF3 (or eRF1 alone), but not post-TCs obtained with puromycin in eRF1's absence...
  8. Alexandrov I, Vishnevskaya A, Ter Avanesyan M, Kushnirov V. Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation. J Biol Chem. 2008;283:15185-92 pubmed publisher
    ..The presence of tyrosines within polyglutamine stretches dramatically enhanced polymer fragmentation and allowed polymer propagation in the absence of Rnq1 and, in some cases, of Hsp104. ..
  9. Masel J, Griswold C. The strength of selection against the yeast prion [PSI+]. Genetics. 2009;181:1057-63 pubmed publisher
    ..If mN(e) > 1, then selection should favor the spread of [PSI(+)] resistance modifiers. In this case, rare conditions where [PSI(+)] is adaptive may permit its persistence in the face of negative selection. ..
  10. Gao H, Zhou Z, Rawat U, Huang C, Bouakaz L, Wang C, et al. RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. Cell. 2007;129:929-41 pubmed
  11. Toyama B, Kelly M, Gross J, Weissman J. The structural basis of yeast prion strain variants. Nature. 2007;449:233-7 pubmed
  12. Newnam G, Birchmore J, Chernoff Y. Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol. 2011;408:432-48 pubmed publisher
    ..Our data demonstrate that heat stress causes asymmetric prion distribution in a cell division and confirm that the effects of Hsps on prions are physiologically relevant. ..
  13. Kryndushkin D, Engel A, Edskes H, Wickner R. Molecular chaperone Hsp104 can promote yeast prion generation. Genetics. 2011;188:339-48 pubmed publisher
    ..The same factor may both enhance de novo prion generation and destabilize existing prion variants, suggesting that prion variants may be selected by changes in the chaperone network. ..
  14. Zhou J, Lancaster L, Trakhanov S, Noller H. Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome. RNA. 2012;18:230-40 pubmed publisher
    ..The rotational movements in the ribosome induced by RF3, and its distinctly different binding orientation to the sarcin-ricin loop of 23S rRNA, raise interesting implications for the mechanism of action of EF-G in translocation. ..
  15. Tyedmers J, Madariaga M, Lindquist S. Prion switching in response to environmental stress. PLoS Biol. 2008;6:e294 pubmed publisher
    ..These findings support the hypothesis that [PSI(+)] is a mechanism to increase survival in fluctuating environments and might function as a capacitor to promote evolvability. ..
  16. Sabate R, Villar Piqué A, Espargaro A, Ventura S. Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules. 2012;13:474-83 pubmed publisher
    ..Overall, we show here that the amyloidogenic pathways of Sup35 and Ure2p prions diverge significantly. ..
  17. Wang H, Duennwald M, Roberts B, Rozeboom L, Zhang Y, Steele A, et al. Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proc Natl Acad Sci U S A. 2008;105:7159-64 pubmed publisher
    ..Our studies provide mechanistic insights and reinvigorate hopes for small-molecule therapies that specifically disrupt intermolecular amyloid contacts. ..
  18. Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller H. Structural basis for translation termination on the 70S ribosome. Nature. 2008;454:852-7 pubmed publisher
    ..Unexpectedly, the main-chain amide group of Gln 230 in the universally conserved GGQ motif of the factor is positioned to contribute directly to peptidyl-tRNA hydrolysis. ..
  19. Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell. 2009;137:146-58 pubmed publisher
    ..The self-perpetuating states of these proteins present a vast source of heritable phenotypic variation that increases the adaptability of yeast populations to diverse environments. ..
  20. de las Heras A, Cain R, Bielecka M, Vazquez Boland J. Regulation of Listeria virulence: PrfA master and commander. Curr Opin Microbiol. 2011;14:118-27 pubmed publisher
    ..Recent work has revealed additional mechanisms that contribute to L. monocytogenes virulence modulation, often via cross-talk with PrfA, or by regulating new genes involved in host colonization. ..
  21. Vivanco Domínguez S, Bueno Martínez J, Leon Avila G, Iwakura N, Kaji A, Kaji H, et al. Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons. J Mol Biol. 2012;417:425-39 pubmed publisher
    ..This is followed by the disassembly of the ribosomal complex of tRNA and mRNA by RRF and elongation factor G. ..
  22. Eliseev B, Kryuchkova P, Alkalaeva E, Frolova L. A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity. Nucleic Acids Res. 2011;39:599-608 pubmed publisher
    ..aediculatus eRF1 to omnipotent mode is due to a single point mutation. Furthermore, we examined the influence of eRF3 on the ability of chimeric and mutant eRF1s to induce peptide release in response to different stop codons. ..
  23. Handa Y, Hikawa Y, Tochio N, Kogure H, Inoue M, Koshiba S, et al. Solution structure of the catalytic domain of the mitochondrial protein ICT1 that is essential for cell vitality. J Mol Biol. 2010;404:260-73 pubmed publisher
    ..In addition, cytochrome c oxidase activity in ICT1 knockdown cells was decreased by 35% compared to that in control cells. These results indicate that ICT1 function is essential for cell vitality and mitochondrial function. ..
  24. Joseph S, Kirkpatrick M. Effects of the [PSI+] prion on rates of adaptation in yeast. J Evol Biol. 2008;21:773-80 pubmed publisher
    ..A major factor affecting the rate of adaptation was initial fitness in the new environment: lines with low initial fitness evolved faster than lines with high initial fitness. ..
  25. Gong H, Romanova N, Allen K, Chandramowlishwaran P, Gokhale K, Newnam G, et al. Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet. 2012;8:e1002634 pubmed publisher
  26. Lekomtsev S, Kolosov P, Bidou L, Frolova L, Rousset J, Kisselev L. Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors. Proc Natl Acad Sci U S A. 2007;104:10824-9 pubmed
  27. Urakov V, Vishnevskaya A, Alexandrov I, Kushnirov V, Smirnov V, Ter Avanesyan M. Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions. Prion. 2010;4:45-52 pubmed
  28. Chauvin C, Jean Jean O. Proteasomal degradation of human release factor eRF3a regulates translation termination complex formation. RNA. 2008;14:240-5 pubmed
  29. Kawai Noma S, Pack C, Tsuji T, Kinjo M, Taguchi H. Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Genes Cells. 2009;14:1045-54 pubmed publisher
    ..The noninvasive methods described here can be applied to other protein-based transmissible systems inside living cells. ..
  30. Inoue Y, Kawai Noma S, Koike Takeshita A, Taguchi H, Yoshida M. Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Genes Cells. 2011;16:545-56 pubmed publisher
    ..Thus, New1 potentially has a regulatory role in prion state in yeast, working independently of the Hsp104 system. ..
  31. Fan Minogue H, Du M, Pisarev A, Kallmeyer A, Salas Marco J, Keeling K, et al. Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination. Mol Cell. 2008;30:599-609 pubmed publisher
    ..These results suggest that the TASNIKS motif and eRF3 function together to trigger eRF1 conformational changes that couple stop codon recognition and peptide release during eukaryotic translation termination...
  32. Eisenreich W, Dandekar T, Heesemann J, Goebel W. Carbon metabolism of intracellular bacterial pathogens and possible links to virulence. Nat Rev Microbiol. 2010;8:401-12 pubmed publisher
    ..Furthermore, we highlight the possible links between intracellular carbon metabolism and the expression of virulence genes. ..
  33. Knowles T, Waudby C, Devlin G, Cohen S, Aguzzi A, Vendruscolo M, et al. An analytical solution to the kinetics of breakable filament assembly. Science. 2009;326:1533-7 pubmed publisher
  34. Crow E, Li L. Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol. 2011;22:452-9 pubmed publisher
    ..In this review, we summarize the characteristics of each prion element, and discuss their potential functional roles in yeast biology. ..
  35. Johnson D, Xu J, Shen Z, Takimoto J, Schultz M, Schmitz R, et al. RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites. Nat Chem Biol. 2011;7:779-86 pubmed publisher
    ..coli tolerates apparent global suppression of UAG. JX33 affords a unique autonomous host for synthesizing and evolving new protein functions by enabling Uaa incorporation at multiple sites. ..
  36. Conard S, Buckley J, Dang M, Bedwell G, Carter R, Khass M, et al. Identification of eRF1 residues that play critical and complementary roles in stop codon recognition. RNA. 2012;18:1210-21 pubmed publisher
    ..In particular, changes in the YCF motif, rather than the TASNIKS motif, correlated most consistently with variant code stop codon selectivity. ..
  37. Kodama H, Ito K, Nakamura Y. The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiae. Genes Cells. 2007;12:639-50 pubmed
    ..These findings suggest that NED functions to switch the functional mode of eRF3 depending on the nature of binding factors. ..
  38. Ivanova E, Kolosov P, Birdsall B, Kelly G, Pastore A, Kisselev L, et al. Eukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis. FEBS J. 2007;274:4223-37 pubmed
  39. Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 2008;27:2712-24 pubmed publisher
    ..This activity is reduced when Ssa1, or enhanced when Ssb1, is incorporated into nascent prions. These findings illuminate several facets of the chaperone interplay that underpins [PSI(+)] inheritance. ..
  40. Atkinson G, Baldauf S, Hauryliuk V. Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evol Biol. 2008;8:290 pubmed publisher
    ..We suggest Ski7p-mediated NSD may be a specialised mechanism for counteracting the effects of increased stop codon read-through caused by prion-domain [PSI+] mediated eRF3 precipitation. ..
  41. Richter R, Rorbach J, Pajak A, Smith P, Wessels H, Huynen M, et al. A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome. EMBO J. 2010;29:1116-25 pubmed publisher
    ..We suggest that ICT1 may be essential for hydrolysis of prematurely terminated peptidyl-tRNA moieties in stalled mitoribosomes. ..
  42. Derdowski A, Sindi S, Klaips C, DISALVO S, Serio T. A size threshold limits prion transmission and establishes phenotypic diversity. Science. 2010;330:680-3 pubmed publisher
    ..Thus, prion conformations may specify phenotypes as population averages in a dynamic system. ..
  43. Nakamura Y, Ito K. tRNA mimicry in translation termination and beyond. Wiley Interdiscip Rev RNA. 2011;2:647-68 pubmed publisher
    ..WIREs RNA 2011 2 647-668 DOI: 10.1002/wrna.81 For further resources related to this article, please visit the WIREs website. ..
  44. Zaher H, Green R. A primary role for release factor 3 in quality control during translation elongation in Escherichia coli. Cell. 2011;147:396-408 pubmed publisher
    ..We conclude that RF3 plays a primary role in vivo in specifying the fidelity of protein synthesis thus impacting overall protein quantity and quality. ..
  45. Becker T, Franckenberg S, Wickles S, Shoemaker C, Anger A, Armache J, et al. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature. 2012;482:501-6 pubmed publisher
    ..Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation...
  46. Kobayashi K, Saito K, Ishitani R, Ito K, Nureki O. Structural basis for translation termination by archaeal RF1 and GTP-bound EF1? complex. Nucleic Acids Res. 2012;40:9319-28 pubmed publisher
    ..We discuss the different mechanisms by which aEF1? recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1?. ..
  47. Bidou L, Allamand V, Rousset J, Namy O. Sense from nonsense: therapies for premature stop codon diseases. Trends Mol Med. 2012;18:679-88 pubmed publisher
    ..Here, we review the molecular basis for PTC readthrough in eukaryotes and describe currently available compounds with significant therapeutic potential for treating genetic disorders and cancer. ..
  48. Santos N, Zhu J, Donohue J, Korostelev A, Noller H. Crystal structure of the 70S ribosome bound with the Q253P mutant form of release factor RF2. Structure. 2013;21:1258-63 pubmed publisher
    ..This rules out proline-induced misfolding and further supports the proposal that catalytic activity requires interaction of the Gln-253 backbone amide with the 3' end of peptidyl-tRNA. ..
  49. Harrison L, Yu Z, Stajich J, Dietrich F, Harrison P. Evolution of budding yeast prion-determinant sequences across diverse fungi. J Mol Biol. 2007;368:273-82 pubmed
    ..Our findings on yeast prion evolution provide further support for the functional significance of these molecules. ..
  50. Chabelskaya S, Gryzina V, Moskalenko S, Le Goff C, Zhouravleva G. Inactivation of NMD increases viability of sup45 nonsense mutants in Saccharomyces cerevisiae. BMC Mol Biol. 2007;8:71 pubmed
    ..In addition, deletion of either UPF2 or UPF3 restored viability of sup45-n double mutants. This is the first demonstration that sup45 mutations do not only change translation fidelity but also acts by causing a change in mRNA stability. ..
  51. Graille M, Chaillet M, van Tilbeurgh H. Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay. J Biol Chem. 2008;283:7145-54 pubmed publisher
  52. Kalastavadi T, True H. Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem. 2008;9:7 pubmed publisher
    ..More importantly, they suggest a mechanism for the observed correlation between age of onset and disease severity with respect to the length of the ORD in humans. ..
  53. Lauer P, Hanson B, Lemmens E, Liu W, Luckett W, Leong M, et al. Constitutive Activation of the PrfA regulon enhances the potency of vaccines based on live-attenuated and killed but metabolically active Listeria monocytogenes strains. Infect Immun. 2008;76:3742-53 pubmed publisher
    ..These results form the basis of a rationale for including the prfA(G155S) allele in future live-attenuated or KBMA L. monocytogenes vaccines advanced to the clinical setting. ..
  54. Roberts B, Duennwald M, Wang H, Chung C, Lopreiato N, Sweeny E, et al. A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat Chem Biol. 2009;5:936-46 pubmed publisher
    ..Thus, synergistic small-molecule combinations that directly eradicate complete strain repertoires likely hold considerable therapeutic potential. ..
  55. Wang Y, Chai B, Wang W, Liang A. Functional characterization of polypeptide release factor 1b in the ciliate Euplotes. Biosci Rep. 2010;30:425-31 pubmed publisher
    ..Bertram, Bell, Ritchie, Fullerton and Stansfield (2000) RNA 6, 1236-1247] and Inagaki et al. [Inagaki, Blouin, Doolittle and Roger (2002) Nucleic Acids Res. 30, 532-544]...
  56. Mathur V, Taneja V, Sun Y, Liebman S. Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast. Mol Biol Cell. 2010;21:1449-61 pubmed publisher
    ..Both [PSI(+)] and [Het-s](y) first appear in daughters as numerous tiny dot-like aggregates, and both require the endocytic protein, Sla2, for ring formation, but not propagation. ..
  57. Lightowlers R, Chrzanowska Lightowlers Z. Terminating human mitochondrial protein synthesis: a shift in our thinking. RNA Biol. 2010;7:282-6 pubmed
  58. Mukai T, Hayashi A, Iraha F, Sato A, Ohtake K, Yokoyama S, et al. Codon reassignment in the Escherichia coli genetic code. Nucleic Acids Res. 2010;38:8188-95 pubmed publisher
    ..Thus, UAG was assigned unambiguously to a natural or non-natural amino acid, according to the specificity of the UAG-decoding tRNA. The result reveals the unexpected flexibility of the genetic code. ..
  59. Xayarath B, VOLZ K, Smart J, Freitag N. Probing the role of protein surface charge in the activation of PrfA, the central regulator of Listeria monocytogenes pathogenesis. PLoS ONE. 2011;6:e23502 pubmed publisher
    ..Our data indicate that the positive charge of the PrfA binding pocket contributes to intracellular activation of PrfA, presumably by facilitating binding of an anionic cofactor. ..
  60. Huynen M, Duarte I, Chrzanowska Lightowlers Z, Nabuurs S. Structure based hypothesis of a mitochondrial ribosome rescue mechanism. Biol Direct. 2012;7:14 pubmed publisher
    ..We hypothesize that mtRF1 recycles such stalled ribosomes, performing a function that is analogous to that of tmRNA in bacteria. ..
  61. Zold k G, Redecke L, Svergun D, Konarev P, Voertler C, Dobbek H, et al. Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies. Nucleic Acids Res. 2007;35:1343-53 pubmed publisher
    ..thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome...
  62. Mukhopadhyay S, Krishnan R, Lemke E, Lindquist S, Deniz A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A. 2007;104:2649-54 pubmed
    ..The stability of such ensembles is likely to play a key role in prion conversion. ..
  63. Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, et al. Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev. 2007;21:3135-48 pubmed
    ..Consequently, PABPC1 binding leads to the activation of Pan2-Pan3 and Caf1-Ccr4. From these results, we suggest a mechanism of mRNA deadenylation by Pan2-Pan3 and Caf1-Ccr4 in cooperation with eRF3 and PABPC1. ..
  64. Bagriantsev S, Gracheva E, Richmond J, Liebman S. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell. 2008;19:2433-43 pubmed publisher
    ..Hsp104, Sis1, and Sse1 interact preferentially with the prion versus nonprion form of Sup35, whereas Sla2 and Ssb1/2 interact with both forms of Sup35 with similar efficiency...
  65. Joseph B, Mertins S, Stoll R, Schär J, Umesha K, Luo Q, et al. Glycerol metabolism and PrfA activity in Listeria monocytogenes. J Bacteriol. 2008;190:5412-30 pubmed publisher
    ..These and other data suggest that the phosphorylation state of PTS permeases correlates with PrfA activity. ..
  66. Weixlbaumer A, Jin H, Neubauer C, Voorhees R, Petry S, Kelley A, et al. Insights into translational termination from the structure of RF2 bound to the ribosome. Science. 2008;322:953-6 pubmed publisher
    ..The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release. ..
  67. Stoll R, Mertins S, Joseph B, Müller Altrock S, Goebel W. Modulation of PrfA activity in Listeria monocytogenes upon growth in different culture media. Microbiology. 2008;154:3856-76 pubmed publisher
    ..The data obtained further support the hypothesis that PrfA activity correlates with the expression level and the phosphorylation state of specific PTS permeases. ..
  68. Bulygin K, Khairulina Y, Kolosov P, Ven yaminova A, Graifer D, Vorobjev Y, et al. Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome. RNA. 2010;16:1902-14 pubmed publisher
    ..Thus, in the A-site-bound state, the eRF1 conformation significantly differs from those in crystals and solution. The model suggested for eRF1 conformation in the ribosomal A site and cross-linking data are compatible. ..
  69. McGlinchey R, Kryndushkin D, Wickner R. Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A. 2011;108:5337-41 pubmed publisher
    ..Our findings give a more realistic picture of the impact of the prion change than does focus on "mild" prion variants. ..
  70. Pisareva V, Skabkin M, Hellen C, Pestova T, Pisarev A. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J. 2011;30:1804-17 pubmed publisher
    ..ABCE1/Pelota/Hbs1 also dissociated vacant 80S ribosomes, which stimulated 48S complex formation, suggesting that Pelota/Hbs1 have an additional role outside of NGD...
  71. Korostelev A. Structural aspects of translation termination on the ribosome. RNA. 2011;17:1409-21 pubmed publisher
    ..In this review, the structural aspects of these mechanisms are discussed. ..
  72. Graille M, Figaro S, Kervestin S, Buckingham R, Liger D, Heurgué Hamard V. Methylation of class I translation termination factors: structural and functional aspects. Biochimie. 2012;94:1533-43 pubmed publisher
    ..However, methylation is catalysed by completely unrelated enzymes. The function of this motif and its post-translational modification will be discussed in the context of recent structural and functional studies. ..
  73. Polshakov V, Eliseev B, Birdsall B, Frolova L. Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1. Protein Sci. 2012;21:896-903 pubmed publisher
    ..Such structural plasticity may be essential for stop codon recognition by human eRF1. ..
  74. Shewmaker F, Wickner R, Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci U S A. 2006;103:19754-9 pubmed
    ..Certain sites in the M domain also exhibit intermolecular distances of approximately 0.5 nm. These results indicate that an in-register parallel beta-sheet structure underlies the [PSI(+)] prion phenomenon. ..
  75. Li X, Yokota T, Ito K, Nakamura Y, Aiba H. Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli. Mol Microbiol. 2007;63:116-26 pubmed
  76. Dong J, Bloom J, Goncharov V, Chattopadhyay M, Millhauser G, Lynn D, et al. Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. J Biol Chem. 2007;282:34204-12 pubmed
    ..It also reveals new features of the yeast prion protein, and provides a level of control over yeast prion assembly that will be useful for future structural studies and for creating amyloid-based biomaterials. ..
  77. Shaw J, Green R. Two distinct components of release factor function uncovered by nucleophile partitioning analysis. Mol Cell. 2007;28:458-67 pubmed
    ..These data lead to a model where RFs make two distinct contributions to catalysis--a relatively nonspecific activation of the catalytic center and specific selection of water as a nucleophile facilitated by Q235. ..
  78. Fan Q, Park K, Du Z, Morano K, Li L. The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. Genetics. 2007;177:1583-93 pubmed
    ..Our findings establish a novel role for Sse1 in [PSI+] de novo formation and variant determination, implying that the mammalian Hsp110 may likewise be involved in the etiology of protein-folding diseases. ..
  79. Youngman E, He S, Nikstad L, Green R. Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release. Mol Cell. 2007;28:533-43 pubmed
    ..We propose that, like other steps in translation, the specificity of peptide release is achieved through an induced-fit mechanism. ..
  80. Zaher H, Green R. Quality control by the ribosome following peptide bond formation. Nature. 2009;457:161-6 pubmed publisher
  81. Shoemaker C, Eyler D, Green R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science. 2010;330:369-72 pubmed publisher
  82. Bulygin K, Khairulina Y, Kolosov P, Ven yaminova A, Graifer D, Vorobjev Y, et al. Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1. Nucleic Acids Res. 2011;39:7134-46 pubmed publisher
    ..These conformations vary by positioning of stop signal purines toward the universally conserved dipeptide 31-GT-32, which neighbors guanines but is oriented more distantly from adenines. ..
  83. Bateman D, Wickner R. [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics. 2012;190:569-79 pubmed publisher
    ..SWI+], a prion of the chromatin remodeling factor Swi1p, was also proposed to benefit its host. We find that none of 70 wild strains carry this prion, suggesting that it is not beneficial. ..
  84. Skabkin M, Skabkina O, Hellen C, Pestova T. Reinitiation and other unconventional posttermination events during eukaryotic translation. Mol Cell. 2013;51:249-64 pubmed publisher
    ..The mobility of posttermination ribosomes suggests that some reinitiation events could involve 80S ribosomes rather than 40S subunits. ..
  85. Zhang Z, Chen H, Bai H, Lai L. Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35. Biophys J. 2007;93:1484-92 pubmed
  86. Chauvin C, Salhi S, Jean Jean O. Human eukaryotic release factor 3a depletion causes cell cycle arrest at G1 phase through inhibition of the mTOR pathway. Mol Cell Biol. 2007;27:5619-29 pubmed
    ..These results strongly suggest that the G1 arrest and the decrease in translation induced by eRF3a depletion are due to the inhibition of mTOR activity and hence that eRF3a belongs to the regulatory pathway of mTOR activity. ..
  87. Miner M, Port G, Bouwer H, Chang J, Freitag N. A novel prfA mutation that promotes Listeria monocytogenes cytosol entry but reduces bacterial spread and cytotoxicity. Microb Pathog. 2008;45:273-81 pubmed publisher
    ..monocytogenes. The prfA Y154C mutant strain may therefore represent a novel attenuated strain of L. monocytogenes for antigen delivery with reduced host cell toxicity. ..
  88. Namy O, Galopier A, Martini C, Matsufuji S, Fabret C, Rousset J. Epigenetic control of polyamines by the prion [PSI+]. Nat Cell Biol. 2008;10:1069-75 pubmed publisher
    ..Antizyme is the first protein to be described for which expression of its functional form is stimulated by [PSI+]. ..
  89. Loh E, Dussurget O, Gripenland J, Vaitkevicius K, Tiensuu T, Mandin P, et al. A trans-acting riboswitch controls expression of the virulence regulator PrfA in Listeria monocytogenes. Cell. 2009;139:770-9 pubmed publisher
    ..Together, our results uncover an unexpected role for riboswitches and a distinct class of regulatory noncoding RNAs in bacteria. ..
  90. Taguchi H, Kawai Noma S. Amyloid oligomers: diffuse oligomer-based transmission of yeast prions. FEBS J. 2010;277:1359-68 pubmed publisher
    ..This review summarizes the topics on the transmissible entities of yeast prions, focusing mainly on the Sup35 protein in [PSI(+)]. ..
  91. Chen B, Bruce K, Newnam G, Gyoneva S, Romanyuk A, Chernoff Y. Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol. 2010;76:1483-99 pubmed publisher
    ..Individual amino acid substitutions within short amyloidogenic stretches drastically alter patterns of cross-species prion conversion, implicating these stretches as major determinants of species specificity. ..
  92. Tank E, Harris D, Desai A, True H. Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol Cell Biol. 2007;27:5445-55 pubmed
    ..Both of these characteristics may contribute to the phenotypic variability associated with PrP repeat expansion diseases. ..