Didehydrophenylalanine, an abundant modification in the beta subunit of plant polygalacturonases.

ABSTRACT: The structure and the activity of proteins are often regulated by transient or stable post- translational modifications (PTM). Different from well-known, abundant modifications such as phosphorylation and glycosylation some modifications are limited to one or a few proteins across a broad range of related species. Although few examples of the latter type are known, the evolutionary conservation of these modifications and the enzymes responsible for their synthesis suggest an important physiological role. Here, the first observation of a new, fold-directing PTM is described. During the analysis of alfalfa cell wall proteins a -2Da mass shift was observed on phenylalanine residues in the repeated tetrapeptide FxxY of the beta-subunit of polygalacturonase. This modular protein is known to be

SUBMITTER: Sergeant K 

PROVIDER: S-EPMC5313189 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature