Recent advances on the post-translational modifications of EXTs and their roles in plant cell walls

Autor: Silvia Melina Velasquez, Juan eSalgado Salter, Bent Larsen ePetersen, Jose Manuel Estevez
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Frontiers in Plant Science, Vol 3 (2012)
Druh dokumentu: article
ISSN: 1664-462X
DOI: 10.3389/fpls.2012.00093
Popis: The genetic set up and the enzymes that define the O-glycosylation sites and transfer the activated sugars to the cell wall protein backbone have remained unknown for a long time. We are now beginning to see the emerging components of the molecular machinery that assembles these complex O-glycoproteins on the plant cell wall. Genes conferring the posttranslational modifications, i.e. proline hydroxylation and subsequent O-glycosylation, of the plant cell wall protein extensin subgroup have being recently identified. In this review we summarize the enzymes that define the O-glycosylation sites on the O-glycoproteins, i.e. the prolyl 4–hydroxylases (P4Hs), the glycosyltransferases that transfer arabinose units (named arabinosyltransferases, AraTs) and the one responsible for the transfer of a single galactose (galactosyltransferase, GalT) on the protein extensin backbones, and finally the EXT peroxidase-mediated crosslinking at the cell wall. We discuss the effect of posttranslational modification on the structure and function of extensins in the plant cell walls.
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