Ancient Ciphers: Translation in Archaea

  title={Ancient Ciphers: Translation in Archaea},
  author={Patrick P. Dennis},

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The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor
The functional characterization of the archaeal homologue, a/eIF2, is reported, which demonstrates that the trimeric factor reconstituted from the recombinant polypeptides has properties similar to those of its eukaryal homologue: it interacts with GTP and Met-tRNAi, and stimulates binding of the latter to the small ribosomal subunit.
Functional Molecular Mapping of Archaeal Translation Initiation Factor 2*
This study characterize the role of each subunit in the binding of the methionylated initiator tRNA and suggests a possible contribution of aIF2α to formation of a productive complex between a IF2 and the small ribosomal subunit is envisaged.
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The data suggest that archaea such as Sulfolobus routinely use two distinct mechanisms for translational initiation, resembling the pathway prevalent in present‐day bacteria, whereas ‘leaderless’ initiation, reminiscent of the eukaryotic pathway, would operate on monocistronic mRNAs and on opening cistrons of polycistronicmRNAs.
Role of aIF5B in archaeal translation initiation
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Recent Advances in Archaeal Translation Initiation
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The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
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Molecular Mechanism of Scanning and Start Codon Selection in Eukaryotes
A robust molecular model now exists, describing the roles of initiation factors, notably eukaryotic initiation factor 1 and eIF1A, in stabilizing an “open” conformation of the 40S subunit with Met-tRNAiMet bound in a low-affinity state conducive to scanning and in triggering rearrangement into a “closed’ conformation incompatible with scanning.


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A strongly conserved mRNA element was identified that is exclusively linked to selenoprotein genes that is located in the 3' untranslated region in six of the mRNAs and in the 5' untranlated region of the fdhA mRNA.
Autogenous translational regulation of the ribosomal MvaL1 operon in the archaebacterium Methanococcus vannielii
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Analysis of the enzyme's ability to cleave tRNA(Trp) substrates lacking exon sequences demonstrated that the mature tRNA-like structure is not required in the substrate, and the possible relationship of this enzyme to other RNA endonucleases is discussed.
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