Antoni R. Slabas

TL;DR: Changes in the extracellular matrix of Arabidopsis thaliana cell suspension cultures following treatments with two fungal pathogen elicitors, chitosan and extracts of Fusarium moniliforme are investigated and spots that represent putative lectin receptor‐like kinase, a putative endochitinase and a XEG possess phosphorylated tyrosine residues are discovered.

TL;DR: The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.

TL;DR: The first crystal structures of an acylated form of ACP from E. coli are determined, that of butyryl-ACP, and it is proposed that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

TL;DR: The observations are best explained by a model in which hooped bundles of microtubules—which are directly or indirectly associated with molecules involved with cellulose biosynthesis at the cell surface—act as an essential template or scaffolding for the orientated deposition of cellulose.

TL;DR: It appears that aspects of speciation reside in the complement of extracellular wall proteins that are absent from their respective cell wall extracts, and the results of the extraction process are indicative of higher order structure.