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  • 1
    Electronic Resource
    Electronic Resource
    In vitro reassembly of active large ribosomal subunits of the halophilic archaebacterium Haloferax mediterranei (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 9256-9261 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00491a021
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  • 2
    Electronic Resource
    Electronic Resource
    Cis-acting signals controlling translational initiation in the thermophilic archaeon Sulfolobus solfataricus (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 34 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In this work, we have studied the in vitro translational features of a bicistronic mRNA of the extremely thermophilic Archaeon Sulfolobus solfataricus, with the aim of determining the nature of the cis-acting signals controlling the recognition of the translation initiation sites in the Archaea. We found that the most important feature for efficient initiation was the presence of a Shine–Dalgarno (SD)-like ribosome-binding motif, whose disruption entirely abolished the translation of the corresponding cistron. The influence of other features, such as the type of initiation codon, was variable and depended upon the gene and its position in the mRNA. However, the translational block caused by the disruption of the SD sequences could be removed by deleting the 5′ untranslated region altogether, thereby creating a ‘leaderless’ mRNA. This suggests that ‘leaderless’ initiation operates by a default mechanism that does not require a specific mRNA–rRNA interaction and may be common to all three primary domains of life.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01615.x
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  • 3
    Electronic Resource
    Electronic Resource
    A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 29 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The chaperonins are high-molecular-weight protein complexes having a characteristic double-ring toroidal shape; they are thought to aid the folding of denatured or newly synthesized polypeptides. These proteins exist as two functionally similar but distantly related families, one including the bacterial and organellar chaperonins and the other (termed the CCT-TRiC family) including the chaperonins of the Archaea and the eukaryotes. The CCT-TRiC chaperonins, particularly their archeal members, are less well known than their bacterial counterparts, and their main cellular function is still doubtful. In this work, we report that the chaperonin of the thermophilic archaeon Sulfolobus solfataricus interacts with several polypeptides other than the two subunits that constitute the 18-mer double-ring structure. We have cloned and sequenced the gene encoding one 90 kDa chaperonin-associated protein and have shown, using biochemical assays, that the product is an enzyme belonging to the family of zinc-dependent aminopeptidases. The Sulfolobus protein shows maximal homology to eukaryotic (yeast and mouse) aminopeptidases. It contains a leucine zipper motif and can be phosphorylated by an unidentified kinase present in the cell extracts. The possible significance of an association between an aminopeptidase and a chaperonin is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00971.x
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  • 4
    Electronic Resource
    Electronic Resource
    Two different mechanisms for ribosome/mRNA interaction in archaeal translation initiation (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 50 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In this study, we have analysed the features of mRNA/ribosome interaction in the thermophilic archeon Sulfolobus solfataricus. Leadered mRNAs endowed with Shine–Dalgarno (SD) motifs formed stable binary complexes with 30S subunits, optimally at high temperature (65–70°C) and without the aid of initiator tRNA (tRNAi) or any factor. ‘Toeprinting’ assays revealed that the SD motifs were necessary and sufficient to direct the 30S subunit to the translation initiation region. Leaderless mRNAs, i.e. mRNAs entirely lacking a 5′-untranslated region (UTR), did not interact directly with 30S subunits but required the presence of tRNAi, indicating that codon–anticodon pairing was required for positioning the ribosome on the initiation codon. The data suggest that archaea such as Sulfolobus routinely use two distinct mechanisms for translational initiation. SD-dependent initiation, resembling the pathway prevalent in present-day bacteria, would operate on distal cistrons of polycistronic mRNAs, whereas ‘leaderless’ initiation, reminiscent of the eukaryotic pathway, would operate on monocistronic mRNAs and on opening cistrons of polycistronic mRNAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03721.x
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  • 5
    Electronic Resource
    Electronic Resource
    The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis (2004)
    [s.l.] : Nature Publishing Group
    Nature medicine 10 (2004), S. 484-486 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The mammalian target of rapamycin, mTOR, regulates cell growth and proliferation. Here we show that the initiation factor of translation (eIF-4E), a downstream effector of mTOR, has oncogenic effects in vivo and cooperates with c-Myc in B-cell lymphomagenesis. We found that c-Myc overrides ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm1042
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  • 6
    Electronic Resource
    Electronic Resource
    Contrast analysis of the composition of ribosomes extracted with different purification procedures (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 33 (2000), S. 1113-1118 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The composition and hydration of E. coli ribosomes isolated with different purification protocols has been analysed by combining two experimental techniques: measurements of small-angle neutron scattering (SANS), for two different isotopic solvent compositions, and refractive index (RI) increments. From the contrast between the solvent and solute scattering densities and the molar polarizability, determined experimentally with SANS and RI measurements, three independent equations are obtained and three unknown quantities are determined: (i) the volume of the solute hydrated skeleton Vs, (ii) the material contained in it, namely the biological components, intrinsic (rRNA and proteins) and extrinsic, such as aminoacylsynthetase and elongation factors, (iii) the number of water molecules structurally bound to the ribosome and non-exchangeable with the solvent. From the form factor at infinite contrast, a second definition of the solute volume is obtained, V_s^c, which represents the volume within the contour surface of the ribosome. This value is generally larger than Vs and can include a certain amount of water molecules, i.e. those inside the volume (V_s^c − Vs). Considering the molar volume of this water to be equal to that of the bulk water, it is possible to evaluate its amount. The particle density calculated from the ribosome components in V_s^c, including proteins, RNA, bound and unbound water molecules, corresponds to the buoyant density measured for E. coli 70S particles. The two ribosomal preparations display different performances in protein synthesis; hence the results indicate that the optimal condition corresponds to a wider skeleton and contour volume but containing a smaller amount of segregated water molecules. It is believed that the method provides a reliable technique to determine the composition of ribosomes under various experimental conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889800006300
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  • 7
    Electronic Resource
    Electronic Resource
    Evolution of translational initiation: new insights from the archaea (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 29 (2005), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Recent in silico and experimental data have shed new light on the mechanism and components of translational initiation in archaea. The available data about the structure of archaeal mRNAs, mRNA/ribosome interaction and archaeal translation initiation factors are reviewed and analyzed in the conceptual framework of the evolution of translational initiation. A model of the initiation step of translation in the Last Universal Common Ancestor of extant cells is presented and discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.fmrre.2004.10.002
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  • 8
    Electronic Resource
    Electronic Resource
    Antibiotic sensitivity of the ribosomes of the ultra-thermophilic archaebacterium Pyrococcus woesei (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 70 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect of several antibiotics on polypeptide synthesis and translational accuracy by ribosomes from the ultra-thermophilic archaebacterium Pyrococcus woesei was investigated. Pyrococcus was found to be unique among the sulfur-dependent extreme thermophiles in being sensitive to the miscoding-inducing action of aminoglycoside antibiotics (except streptomycin). On the whole, the antibiotic sensitivity patterns indicate phylogenetic closeness of Pyrococcus to the methanogenic-halophilic branch of the archaebacterial tree.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb13990.x
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  • 9
    Electronic Resource
    Electronic Resource
    In vitro translation of archaeal natural mRNAs at high temperature (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 107 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Efficient in vitro translation of archaeal natural mRNAs at high (75°C) temperature has been achieved by employing either crude cell lysates or purified ribosomes and soluble proteins of the extreme thermophile Sulfolobus solfataricus. The features of the system are described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06009.x
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  • 10
    Electronic Resource
    Electronic Resource
    Intralineage diversity of archaebacterial ribosomes: A dichotomy of ribosome features separates sulfur-dependent archaebacteria and methanococcaceae from other archaebacterial taxa (1986)
    Springer
    Journal of molecular evolution 23 (1986), S. 343-353 
    Details
    ISSN: 1432-1432
    Keywords: Archaebacteria ; Ribosomes ; Methanogens ; Halophiles ; Sulfur-dependent thermophiles ; Eubacteria ; Eukaryotes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The aggregate masses and relative protein contents of eubacterial and archaebacterial ribosomes have been estimated from the buoyant densities of the ribosomal subunits and the anhydrous weights of the rRNA species. In contrast to the situation in eubacteria, archaebacterial ribosomes fall into two size classes that differ only in the relative abundances of their protein moieties. One class comprises eubacterial-sized particles (2.3-megadalton (Mdal) monomer; 1.5-Mdal and 0.8-Mdal large and small subunits, respectively) having a “eubacterial” composition of roughly one-third protein and two-thirds RNA. The other class comprises ribosomes heavier than those of eubacteria (3-Mdal monomer; 1.8-Mdal and 1.2-Mdal subunits) and having the same protein/RNA ratio as eukaryotic ribosomes (55% and 50% protein for the small and large subunits, respectively). Eubacterialsized ribosomes are harbored by extreme halophiles and all methanogens but the Methanococcaceae. Ribosomes heavier than those of eubacteria are found in the Methanococcaceae and all sulfur-dependent thermophiles. The data indicate that a change in ribosome structure occurred within the “methanogen” branch; therefore, although ribosome composition is distributed in archaebacteria, its distribution does not break them into two separate kingdoms: The Methanococcaceae and Methanobacteriaceae are related to each other far more closely than either is to the sulfur-dependent thermophiles, and the root of the archaebacterial tree definitely does not lie betweenMethanobacterium andMethanococcus. We surmise that ribosomes larger than those of eubacteria represent a more rudimentary organelle structure that became fixed owing to nonparallel evolution of the translational machinery in archaebacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02100644
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