ABSTRACT
Pollen apertures are an interesting model for the formation of specialized plasma-membrane domains. The plant-specific protein INP1 serves as a key aperture factor in such distantly related species as Arabidopsis, rice and maize. Although INP1 orthologues probably play similar roles throughout flowering plants, they show substantial sequence divergence and often cannot substitute for each other, suggesting that INP1 might require species-specific partners. Here, we present a new aperture factor, INP2, which satisfies the criteria for being a species-specific partner for INP1. Both INP proteins display similar structural features, including the plant-specific DOG1 domain, similar patterns of expression and mutant phenotypes, as well as signs of co-evolution. These proteins interact with each other in a species-specific manner and can restore apertures in a heterologous system when both are expressed but not when expressed individually. Our findings suggest that the INP proteins form a species-specific functional module that underlies formation of pollen apertures.
Subject(s)
Arabidopsis/growth & development , Oryza/growth & development , Plant Proteins/metabolism , Pollen/anatomy & histology , Pollen/growth & development , Pollen/genetics , Zea mays/growth & development , Arabidopsis/anatomy & histology , Arabidopsis/genetics , Cell Wall/genetics , Cell Wall/metabolism , Crops, Agricultural/anatomy & histology , Crops, Agricultural/genetics , Crops, Agricultural/growth & development , Gene Expression Regulation, Plant , Genes, Plant , Genetic Variation , Genotype , Mutation , Oryza/anatomy & histology , Oryza/genetics , Phenotype , Plant Proteins/genetics , Species Specificity , Zea mays/anatomy & histology , Zea mays/geneticsABSTRACT
The functional organization of the plant nuclear envelope is gaining increasing attention through new connections made between nuclear envelope-associated proteins and important plant biological processes. Animal nuclear envelope proteins play roles in nuclear morphology, nuclear anchoring and movement, chromatin tethering and mechanical signaling. However, how these roles translate to functionality in a broader biological context is often not well understood. A surprising number of plant nuclear envelope-associated proteins are plant-unique, suggesting that separate functionalities evolved after the split of Opisthokonta and Streptophyta. Significant progress has now been made in discovering broader biological roles of plant nuclear envelope proteins, increasing the number of known plant nuclear envelope proteins, and connecting known proteins to chromatin organization, gene expression, and the regulation of nuclear calcium. The interaction of viruses with the plant nuclear envelope is another emerging theme. Here, we survey the recent developments in this still relatively new, yet rapidly advancing field.
