The influence of metabolically engineered glucosinolates profiles in Arabidopsis thaliana on Plutella xylostella preference and performance

The oviposition preference and larval performance of the diamondback moth (DBM), Plutella xylostella, was studied using Arabidopsis thaliana plants with modified glucosinolate (GS) profiles containing novel GSs as a result of the introduction of individual CYP79 genes. The insect parameters were determined in a series of bioassays. The GS content of the plants as well as the number of trichomes were measured. Multivariate analysis was used to determine the possible relationships among insect and plant variables. The novel GSs in the tested lines did not appear to have any unequivocal effect on the DBM. Instead, the plant characteristics that affected larval performance and larval preference did not influence oviposition preference. Trichomes did not affect oviposition, but influenced larval parameters negatively. Although the tested A. thaliana lines had earlier been shown to influence disease resistance, in this study no clear results were found for P. xylostella

The Chromodomain of LIKE HETEROCHROMATIN PROTEIN 1 Is Essential for H3K27me3 Binding and Function during Arabidopsis Development

Polycomb group (PcG) proteins are essential to maintain gene expression patterns during development. Transcriptional repression by PcG proteins involves trimethylation of H3K27 (H3K27me3) by Polycomb Repressive Complex 2 (PRC2) in animals and plants. PRC1 binds to H3K27me3 and is required for transcriptional repression in animals, but in plants PRC1-like activities have remained elusive. One candidate protein that could be involved in PRC1-like functions in plants is LIKE HETEROCHROMATIN PROTEIN 1 (LHP1), because LHP1 associates with genes marked by H3K27me3 in vivo and has a chromodomain that binds H3K27me3 in vitro. Here, we show that disruption of the chromodomain of Arabidopsis thaliana LHP1 abolishes H3K27me3 recognition, releases gene silencing and causes similar phenotypic alterations as transcriptional lhp1 null mutants. Therefore, binding to H3K27me3 is essential for LHP1 protein function