Structural and functional characterization of annexin 1 from Medicago truncatula
Copyright © 2013 Elsevier Masson SAS. All rights reserved.
| Publié dans: | Plant physiology and biochemistry : PPB. - 1991. - 73(2013) vom: 05. Dez., Seite 56-62 |
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| Auteur principal: | |
| Autres auteurs: | , , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2013
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| Accès à la collection: | Plant physiology and biochemistry : PPB |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't 3-D AnnAt1–AnnAt8 AnnMt1–AnnMt9 Annexin 1 AnxA1–A11 and AnxA13 CVs Ion channel Medicago truncatula plus... |
| Résumé: | Copyright © 2013 Elsevier Masson SAS. All rights reserved. Annexins are calcium- and membrane-binding proteins that have been shown to have diverse properties such as actin, integrin and GTP binding, both in animals and plants. Recently, Medicago truncatula annexin 1 (AnnMt1) has been suggested to participate in nodulation (Nod factor signaling) and mycorrhization in legume plants. In this report we demonstrate for the first time that recombinant AnnMt1 (rec-AnnMt1) mediates membrane permeabilization to cations with conductance ranging from 16 pS to 329 pS. In agreement with other structurally determined annexins, homology modeling of AnnMt1 suggests that most of the functional determinants are found on the convex surface of the modeled structure. In conclusion, we propose a potential constitutive role of AnnMt1 in Nod factor signaling as a non-specific ion channel |
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| Description: | Date Completed 29.07.2014 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2690 |
| DOI: | 10.1016/j.plaphy.2013.08.010 |