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Margarida Saramago1, Marta Robledo2, Rute G Matos1

  • 1Instituto de Tecnología Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.

Frontiers in Genetics
|September 14, 2018
PubMed
Summary

We characterized RNase III from Sinorhizobium meliloti (SmRNase III), a metal-dependent enzyme crucial for RNA processing. SmRNase III impacts bacterial symbiosis, affecting nodulation and nitrogen fixation in plants.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Ribonuclease (RNase) III enzymes are essential metal-dependent endoribonucleases involved in RNA processing and interference.
  • Eukaryotic RNase III enzymes like Dicer and Drosha play critical roles in RNA silencing pathways.
  • Understanding bacterial RNase III enzymes provides insights into fundamental biological processes.

Purpose of the Study:

  • To characterize the RNase III enzyme from the symbiotic nitrogen-fixing bacterium Sinorhizobium meliloti (SmRNase III).
  • To elucidate the biochemical properties and catalytic mechanism of SmRNase III.
  • To investigate the biological role of SmRNase III in S. meliloti and its symbiotic interaction with plants.

Main Methods:

  • Purification and biochemical characterization of recombinant SmRNase III.
Keywords:
RNA degradationSinorhizobium melilotiendoribonucleasesribonuclease IIIsymbiosis

Related Experiment Videos

  • Enzyme activity assays using structured RNA substrates and varying metal cofactors.
  • Site-directed mutagenesis to investigate the role of key amino acids in catalysis.
  • Analysis of SmRNase III loss-of-function mutants in S. meliloti regarding growth, nodulation, and nitrogen fixation.

    • Main Results:

    • Purified SmRNase III is a metal-dependent double-strand specific endoribonuclease that dimerizes.
    • SmRNase III exhibits distinct catalytic features compared to EcRNase III, preferring Mn2+ and requiring higher cofactor concentrations.
    • The enzyme is involved in 23S rRNA maturation and degrades various endogenous RNAs.
    • Loss of SmRNase III function affects S. meliloti growth, nodulation kinetics, and symbiotic nitrogen fixation efficiency.

    Conclusions:

    • SmRNase III is a unique RNase III enzyme with specific biochemical properties.
    • SmRNase III plays a significant role in the symbiotic relationship between S. meliloti and its legume host.
    • The enzyme's function impacts nodulation and nitrogen fixation, influencing plant growth and development.