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A Redox-Sensitive Cysteine Is Required for PIN1At Function.

Benjamin Selles1, Tiphaine Dhalleine1, Alexis Boutilliat1

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|January 3, 2022
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The cysteine residue in Arabidopsis PIN1At is essential for its peptidyl-prolyl isomerase (PPIase) activity and protein folding regulation. Oxidative stress can modify this cysteine, potentially impacting enzyme function.

Keywords:
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Parvulins are essential peptidyl-prolyl isomerases (PPIases) involved in protein folding and regulation.
  • Arabidopsis PIN1At, human PIN1, and yeast ESS1 are parvulin members sharing a conserved cysteine residue.
  • PIN1At lacks an N-terminal WW domain present in other parvulins.

Purpose of the Study:

  • To investigate the role of the cysteine residue in Arabidopsis PIN1At catalysis.
  • To determine if the cysteine residue is subject to oxidative modifications.
  • To explore the functional significance of cysteine modifications in PIN1At activity.

Main Methods:

  • Functional complementation of yeast ess1 mutant.
  • In vitro PPIase activity assays.
  • Hydrogen peroxide (H2O2) treatment and oxidation studies.
  • Analysis of cysteine modifications (dimerization, sulfinic/sulfonic acid formation).

Main Results:

  • Cysteine at position 69 is mandatory for PIN1At function in vivo, with substitution by Asppartially rescuing activity.
  • Non-functional cysteinic variants showed decreased in vitro PPIase activity.
  • H2O2 treatment reduced PIN1At activity, with Cys69 oxidation leading to dimers or oxidized forms.
  • Thioredoxins reduced the disulfide bond formation.

Conclusions:

  • The sole cysteine residue in PIN1At is critical for its catalytic activity.
  • Reversible disulfide bond formation involving Cys69 may serve as a regulatory or protective mechanism under oxidative stress.
  • Oxidative modifications of Cys69 can alter PIN1At function.