Conserved residues in the ankyrin domain of VAPYRIN indicate potential protein-protein interaction surfaces
- Feddermann, Nadja Department of Biology, University of Fribourg, Fribourg, Switzerland
- Reinhardt, Didier Department of Biology, University of Fribourg, Fribourg, Switzerland
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27.01.2011
Published in:
- Plant Signaling & Behavior. - 2011, vol. 6, no. 5, p. 680-684
English
Plant VAPYRINS are required for the establishment of arbuscular mycorrhiza (AM) and root nodule symbiosis (RNS). In vapyrin mutants, the intracellular accommodation of AM fungi and rhizobia is blocked, and in the case of AM, the fungal endosymbiont cannot develop arbuscules which serve for nutrient exchange. VAPYRINs are plant-specific proteins that consists of a major sperm protein (MSP) domain and an ankyrin domain. Comparison of VAPYRINS of dicots, monocots, and the moss Physcomitrella patens reveals a highly conserved domain structure. We focused our attention on the ankyrin domain, which closely resembles the D34 domain of human ankyrin R. Conserved residues within the petunia VAPYRIN cluster to a surface patch on the concave side of the crescent-shaped ankyrin domain, suggesting that this region may represent a conserved binding site involved in the formation of a protein complex with an essential function in intracellular accommodation of microbial endosymbionts.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 27907
- DOI 10.4161/psb.6.5.14972
- Persistent URL
- https://folia.unifr.ch/unifr/documents/302229
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