Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions
Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases...
Main Authors: | , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2018-09-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | http://www.mdpi.com/1422-0067/19/10/2876 |
id |
doaj-55b2bc46914f4a579bd577a1a2336198 |
---|---|
record_format |
Article |
spelling |
doaj-55b2bc46914f4a579bd577a1a23361982020-11-25T00:47:08ZengMDPI AGInternational Journal of Molecular Sciences1422-00672018-09-011910287610.3390/ijms19102876ijms19102876Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting FunctionsSabine Lüthje0Teresa Martinez-Cortes1Oxidative Stress and Plant Proteomics Group, Institute for Plant Science and Microbiology, University of Hamburg, Ohnhorststrasse 18, 22609 Hamburg, GermanyDpto de Biología Animal, Biología Vegetal y Ecología (Lab. Fisiología Vegetal), Facultad de Ciencias—Universidade da Coruña, A Zapateira s/n, 15071 A Coruña, SpainClass III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.http://www.mdpi.com/1422-0067/19/10/2876Arabidopsis thalianaClass III peroxidaseMedicago truncatulamicrodomainsphylogeneticsplasma membraneprotein–protein interactionOryza sativatonoplastZea mays |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sabine Lüthje Teresa Martinez-Cortes |
spellingShingle |
Sabine Lüthje Teresa Martinez-Cortes Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions International Journal of Molecular Sciences Arabidopsis thaliana Class III peroxidase Medicago truncatula microdomains phylogenetics plasma membrane protein–protein interaction Oryza sativa tonoplast Zea mays |
author_facet |
Sabine Lüthje Teresa Martinez-Cortes |
author_sort |
Sabine Lüthje |
title |
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions |
title_short |
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions |
title_full |
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions |
title_fullStr |
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions |
title_full_unstemmed |
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions |
title_sort |
membrane-bound class iii peroxidases: unexpected enzymes with exciting functions |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2018-09-01 |
description |
Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics. |
topic |
Arabidopsis thaliana Class III peroxidase Medicago truncatula microdomains phylogenetics plasma membrane protein–protein interaction Oryza sativa tonoplast Zea mays |
url |
http://www.mdpi.com/1422-0067/19/10/2876 |
work_keys_str_mv |
AT sabineluthje membraneboundclassiiiperoxidasesunexpectedenzymeswithexcitingfunctions AT teresamartinezcortes membraneboundclassiiiperoxidasesunexpectedenzymeswithexcitingfunctions |
_version_ |
1725261674190995456 |