A novel three-unit tRNA splicing endonuclease found in ultrasmall Archaea possesses broad substrate specificity. (Articolo in rivista)

Type
Label
  • A novel three-unit tRNA splicing endonuclease found in ultrasmall Archaea possesses broad substrate specificity. (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • Fujishima K, Sugahara J, Miller CS, Baker BJ, Di Giulio M, Takesue K, Sato A, Tomita M, Banfield JF, Kanai A. (2011)
    A novel three-unit tRNA splicing endonuclease found in ultrasmall Archaea possesses broad substrate specificity.
    in Nucleic acids research
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Fujishima K, Sugahara J, Miller CS, Baker BJ, Di Giulio M, Takesue K, Sato A, Tomita M, Banfield JF, Kanai A. (literal)
Rivista
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  • PMID: 21880595 e-pub (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Pubblicazione (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • CNR-IGB \"ABT\" (literal)
Titolo
  • A novel three-unit tRNA splicing endonuclease found in ultrasmall Archaea possesses broad substrate specificity. (literal)
Abstract
  • RNA splicing endonucleases, essential enzymes found in Archaea and Eukaryotes, are involved in the processing of pre-tRNA molecules. In Archaea, three types of splicing endonuclease [homotetrameric: ±(4), homodimeric: ±(2), and heterotetrameric: (±²)(2)] have been identified, each representing different substrate specificity during the tRNA intron cleavage. Here, we discovered a fourth type of archaeal tRNA splicing endonuclease (µ(2)) in the genome of the acidophilic archaeon Candidatus Micrarchaeum acidiphilum, referred to as ARMAN-2 and its closely related species, ARMAN-1. The enzyme consists of two duplicated catalytic units and one structural unit encoded on a single gene, representing a novel three-unit architecture. Homodimeric formation was confirmed by cross-linking assay, and site-directed mutagenesis determined that the conserved L10-pocket interaction between catalytic and structural unit is necessary for the assembly. A tRNA splicing assay reveal that µ(2) endonuclease cleaves both canonical and non-canonical bulge-helix-bulge motifs, similar to that of (±²)(2) endonuclease. Unlike other ARMAN and Euryarchaeota, tRNAs found in ARMAN-2 are highly disrupted by introns at various positions, which again resemble the properties of archaeal species with (±²)(2) endonuclease. Thus, the discovery of µ(2) endonuclease in an archaeon deeply branched within Euryarchaeota represents a new example of the coevolution of tRNA and their processing enzymes. (literal)
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