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Cold adaptation in DEAD-box proteins.

Gwendoline Cartier1, Florence Lorieux, Frédéric Allemand

  • 1CNRS UPR9073, University Paris VII, Institut de Biologie Physico-chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.

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Cold-adapted DEAD-box proteins in bacteria exhibit distinct enzymatic properties. Psychrophilic SrmB shows lower ATPase activation energy, while RhlE has cold-adapted RNA unwinding, suggesting varied roles in RNA metabolism at low temperatures.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • RNA structures require dynamic rearrangements, even at low temperatures in psychrophilic organisms.
  • DEAD-box proteins are RNA-dependent ATPases with helicase activity, crucial for in vivo RNA rearrangements.
  • Understanding cold adaptation mechanisms of these proteins is vital for psychrophilic biology.

Purpose of the Study:

  • To compare the enzymatic properties of Escherichia coli DEAD-box proteins (SrmB and RhlE) with their orthologs from psychrophilic bacteria (Pseudoalteromonas haloplanktis and Colwellia psychrerythraea).
  • To investigate the cold adaptation strategies of these DEAD-box proteins and infer their in vivo functions.

Main Methods:

  • Comparative analysis of ATPase and RNA unwinding activities of mesophilic and psychrophilic DEAD-box proteins.
  • Determination of activation energies for enzymatic activities at different temperatures.
  • In vitro biochemical assays to characterize protein function.

Main Results:

  • Psychrophilic SrmB exhibits lower activation energy for ATPase activity compared to its mesophilic counterpart, enhancing activity at low temperatures.
  • Psychrophilic RhlE shows reduced activation energy for RNA unwinding activity, indicating cold adaptation in its helicase function.
  • RhlE demonstrates significantly higher in vitro helicase activity than SrmB.

Conclusions:

  • Different cold adaptation modes in SrmB (ATPase activity) and RhlE (RNA unwinding) suggest distinct in vivo roles: ATP-dependent RNA binding for SrmB and RNA helicase for RhlE.
  • Cold-adapted RNA helicases like RhlE are likely essential for facilitating RNA metabolism in psychrophilic bacteria.
  • These findings highlight the functional diversification of DEAD-box proteins in response to environmental temperature.