Abstract
The genetic set up and the enzymes that define the O-glycosylation sites and transfer the activated sugars to cell wall glycoprotein Extensins (EXTs) 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 EXTs have been 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 transferring a single galactose (galactosyltransferase, GalT) on the protein EXT backbones. We discuss the effects of posttranslational modifications on the structure and function of extensins in plant cell walls.
Original language | English |
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Article number | 93 |
Journal | Frontiers in Plant Science |
Volume | 3 |
Issue number | MAY |
DOIs | |
Publication status | Published - 15 May 2012 |
Externally published | Yes |
Keywords
- Cell expansion
- Extensins
- O-glycoproteins
- O-glycosylation
- Plant cell wall
- Proline hydroxylation
ASJC Scopus subject areas
- Plant Science