Craterostigma plantagineum cell wall composition is remodelled during desiccation and the glycine-rich protein CpGRP1 interacts with pectins through clustered arginines.

Craterostigma plantagineum cell wall desiccation tolerance glycine-rich protein leaf folding lipid binding pectin phosphatidic acid resurrection plant

Journal

The Plant journal : for cell and molecular biology
ISSN: 1365-313X
Titre abrégé: Plant J
Pays: England
ID NLM: 9207397

Informations de publication

Date de publication:
11 2019
Historique:
received: 21 03 2019
revised: 27 06 2019
accepted: 23 07 2019
pubmed: 28 7 2019
medline: 21 7 2020
entrez: 28 7 2019
Statut: ppublish

Résumé

Craterostigma plantagineum belongs to the desiccation-tolerant angiosperm plants. Upon dehydration, leaves fold and the cells shrink which is reversed during rehydration. To understand this process changes in cell wall pectin composition, and the role of the apoplastic glycine-rich protein 1 (CpGRP1) were analysed. Cellular microstructural changes in hydrated, desiccated and rehydrated leaf sections were analysed using scanning electron microscopy. Pectin composition in different cell wall fractions was analysed with monoclonal antibodies against homogalacturonan, rhamnogalacturonan I, rhamnogalacturonan II and hemicellulose epitopes. Our data demonstrate changes in pectin composition during dehydration/rehydration which is suggested to affect cell wall properties. Homogalacturonan was less methylesterified upon desiccation and changes were also demonstrated in the detection of rhamnogalacturonan I, rhamnogalacturonan II and hemicelluloses. CpGRP1 seems to have a central role in cell adaptations to water deficit, as it interacts with pectin through a cluster of arginine residues and de-methylesterified pectin presents more binding sites for the protein-pectin interaction than to pectin from hydrated leaves. CpGRP1 can also bind phosphatidic acid (PA) and cardiolipin. The binding of CpGRP1 to pectin appears to be dependent on the pectin methylesterification status and it has a higher affinity to pectin than its binding partner CpWAK1. It is hypothesised that changes in pectin composition are sensed by the CpGRP1-CpWAK1 complex therefore leading to the activation of dehydration-related responses and leaf folding. PA might participate in the modulation of CpGRP1 activity.

Identifiants

pubmed: 31350933
doi: 10.1111/tpj.14479
doi:

Substances chimiques

Phosphatidic Acids 0
Plant Proteins 0
rhamnogalacturonan I 0
rhamnogalacturonan II 0
Pectins 89NA02M4RX
Arginine 94ZLA3W45F
polygalacturonic acid VV3XD4CL04

Banques de données

GENBANK
['ALQ43973.1', 'KT893872.1']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

661-676

Commentaires et corrections

Type : CommentIn

Informations de copyright

© 2019 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.

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Auteurs

Niklas U Jung (NU)

Institute of Molecular Physiology and Biotechnology of Plants (IMBIO), Faculty of Natural Sciences, University of Bonn, Kirschallee 1, Bonn, D-53115, Germany.

Valentino Giarola (V)

Institute of Molecular Physiology and Biotechnology of Plants (IMBIO), Faculty of Natural Sciences, University of Bonn, Kirschallee 1, Bonn, D-53115, Germany.

Peilei Chen (P)

Institute of Molecular Physiology and Biotechnology of Plants (IMBIO), Faculty of Natural Sciences, University of Bonn, Kirschallee 1, Bonn, D-53115, Germany.

John Paul Knox (JP)

Centre for Plant Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.

Dorothea Bartels (D)

Institute of Molecular Physiology and Biotechnology of Plants (IMBIO), Faculty of Natural Sciences, University of Bonn, Kirschallee 1, Bonn, D-53115, Germany.

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