Conserved residues in the ankyrin domain of VAPYRIN indicate potential protein-protein interaction surfaces

被引：15

作者：

Feddermann, Nadja ^{[1
]}

Reinhardt, Didier ^{[1
]}

机构：

[1] Dept Biol, Fribourg, Switzerland

来源：

PLANT SIGNALING & BEHAVIOR | 2011年 / 6卷 / 05期

关键词：

VAPYRIN; arbuscular mycorrhiza; petunia; symbiosis; glomus; ankyrin; major sperm protein; VAP;

D O I：

10.4161/psb.6.5.14972

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：680 / 684

页数：5

共 16 条

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