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MINI REVIEW article

Front. Plant Sci.
Sec. Plant Proteomics and Protein Structural Biology
Volume 15 - 2024 | doi: 10.3389/fpls.2024.1487328
This article is part of the Research Topic Thiol-Based Redox Regulation and Signaling View all articles

The ascorbate peroxidase-related protein: insights into its functioning in Chlamydomonas and Arabidopsis

Provisionally accepted
Anna Caccamo Anna Caccamo 1,2,3Fernanda Lazzarotto Fernanda Lazzarotto 4MARCIA MARGIS-PINHEIRO MARCIA MARGIS-PINHEIRO 4Joris Messens Joris Messens 2,3Claire Remacle Claire Remacle 1*
  • 1 University of Liège, Liège, Belgium
  • 2 VIB-VUB Center for Structural Biology, Vrije University Brussel, Brussels, Brussels, Belgium
  • 3 Brussels Center for Redox Biology (BCRB), Brussels, Belgium
  • 4 Federal University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul, Brazil

The final, formatted version of the article will be published soon.

    We review the newly classified ascorbate peroxidase-related proteins (APX-R), which do not use ascorbate as electron donor to scavenge H2O2. We summarize recent discoveries on the function and the characterization of the APX-R protein of the green unicellular alga Chlamydomonas reinhardtii and the land plant Arabidopsis thaliana. Additionally, we conduct in silico analyses on the conserved MxxM motif, present in most of the APX-R protein in different organisms, which is proposed to bind copper. Based on these analyses, we discuss the similarities between the APX-R and the Class III peroxidases.

    Keywords: Chlamydomonas, Arabidopsis, APX-R, H2O2, phylogeny. (Min.5-Max. 8

    Received: 27 Aug 2024; Accepted: 17 Sep 2024.

    Copyright: © 2024 Caccamo, Lazzarotto, MARGIS-PINHEIRO, Messens and Remacle. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Claire Remacle, University of Liège, Liège, Belgium

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