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    Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates

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    Characterization of Aquifex ...
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    Genre
    Journal Article
    Date
    2011-04-01
    Author
    Shi, Z
    Nicholson, RH
    Jaggi, R
    Nicholson, AW
    Subject
    Amino Acid Sequence
    Bacteria
    Base Pairing
    Base Sequence
    Biocatalysis
    Cations, Divalent
    Enzyme Stability
    Glutamine
    Hydrogen-Ion Concentration
    Molecular Sequence Data
    RNA Precursors
    RNA, Bacterial
    RNA, Double-Stranded
    RNA, Ribosomal
    RNA, Ribosomal, 16S
    RNA, Ribosomal, 23S
    Ribonuclease III
    Salts
    Temperature
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    Permanent link to this record
    http://hdl.handle.net/20.500.12613/5532
    
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    DOI
    10.1093/nar/gkq1030
    Abstract
    Ribonuclease III cleaves double-stranded (ds) structures in bacterial RNAs and participates in diverse RNA maturation and decay pathways. Essential insight on the RNase III mechanism of dsRNA cleavage has been provided by crystallographic studies of the enzyme from the hyperthermophilic bacterium, Aquifex aeolicus. However, the biochemical properties of A. aeolicus (Aa)-RNase III and the reactivity epitopes of its substrates are not known. The catalytic activity of purified recombinant Aa-RNase III exhibits a temperature optimum of ∼70-85°C, with either Mg2+ or Mn2+ supporting efficient catalysis. Small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. Structural studies have shown that a conserved glutamine (Q157) in the Aa-RNase III dsRNA-binding domain (dsRBD) directly interacts with a proximal box base pair. Aa-RNase III cleavage of the pre-16S substrate is blocked by the Q157A mutation, which reflects a loss of substrate binding affinity. Thus, a highly conserved dsRBD-substrate interaction plays an important role in substrate recognition by bacterial RNase III. © 2011 The Author(s).
    Citation to related work
    Oxford University Press (OUP)
    Has part
    Nucleic Acids Research
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/5514
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