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Showing 1–5 of 5 results
Advanced filters: Author: Paul Gollnick Clear advanced filters

  • The crystal structure of the trp RNA-binding attenuation protein of Bacillus subtilis solved at 1.8 Å resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit β-sheets to form a β-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent β-sheets in the β-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.

    • Alfred A. Antson
    • John Otridge
    • Paul Gollnick
    Research
    Nature
    Volume: 374, P: 693-700

  • Aberrant RNA editing is linked to a range of neuropsychiatric and chronic diseases. Here Sharma et al. show that APOBEC3A can function as an RNA editing protein in response to physiological stimuli, significantly expanding our understanding of RNA editing and the role this may play in diseases.

    • Shraddha Sharma
    • Santosh K. Patnaik
    • Bora E. Baysal
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-15

  • Repeating RNA sequences often serve as protein targets during regulatory processes involving single-stranded RNA (ssRNA). New data on the HutP protein show how it is activated and binds a repeat-containing ssRNA. Together with previous work, these studies demonstrate the versatility of RNA-binding proteins in regulating transcription in bacteria.

    • Paul Gollnick
    • Alfred Antson
    News & Views
    Nature Structural & Molecular Biology
    Volume: 12, P: 289-290