VAMP721a and VAMP721d are important for pectin dynamics and release of bacteria in soybean nodules

© 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1990. - 210(2016), 3 vom: 15. Mai, Seite 1011-21
1. Verfasser: Gavrin, Aleksandr (VerfasserIn)
Weitere Verfasser: Chiasson, David, Ovchinnikova, Evgenia, Kaiser, Brent N, Bisseling, Ton, Fedorova, Elena E
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't endosymbiosis exocytosis intracellular infection legume-rhizobia symbiosis plant cell wall soybean Plant Proteins Pectins mehr... 89NA02M4RX Cellulose 9004-34-6 Polysaccharide-Lyases EC 4.2.2.- pectate lyase EC 4.2.2.2
Beschreibung
Zusammenfassung:© 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.
In root nodules rhizobia enter host cells via infection threads. The release of bacteria to a host cell is possible from cell wall-free regions of the infection thread. We hypothesized that the VAMP721d and VAMP721e exocytotic pathway, identified before in Medicago truncatula, has a role in the local modification of cell wall during the release of rhizobia. To clarify the role of VAMP721d and VAMP721e we used Glycine max, a plant with a determinate type of nodule. The localization of the main polysaccharide compounds of primary cell walls was analysed in control vs nodules with partially silenced GmVAMP721d. The silencing of GmVAMP721d blocked the release of rhizobia. Instead of rhizobia-containing membrane compartments - symbiosomes - the infected cells contained big clusters of bacteria embedded in a matrix of methyl-esterified and de-methyl-esterified pectin. These clusters were surrounded by a membrane. We found that GmVAMP721d-positive vesicles were not transporting methyl-esterified pectin. We hypothesized that they may deliver the enzymes involved in pectin turnover. Subsequently, we found that GmVAMP721d is partly co-localized with pectate lyase. Therefore, the biological role of VAMP721d may be explained by its action in delivering pectin-modifying enzymes to the site of release
Beschreibung:Date Completed 26.12.2016
Date Revised 09.01.2024
published: Print-Electronic
GENBANK: X15061
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.13837