Cellular and Molecular Life Sciences CMLS

, Volume 58, Issue 10, pp 1386–1398

Synthetic genes for the elucidation of glycosylation codes for arabinogalactan-proteins and other hydroxyproline-rich glycoproteins

  • M.J. Kieliszewski
  • E. Shpak

DOI: 10.1007/PL00000783

Cite this article as:
Kieliszewski, M. & Shpak, E. CMLS, Cell. Mol. Life Sci. (2001) 58: 1386. doi:10.1007/PL00000783

Abstract.

Hydroxyproline-rich glycoproteins (HRGPs) are ubiquitous architectural components of the growing plant cell wall, accounting for as much as 10-20% of the dry weight. HRGPs are implicated in all aspects of plant growth and development, including responses to stress. The HRGP superfamily contains three major groups which represent a continuum of peptide periodicity and hydroxyproline-O-glycosylation. These groups range from the highly periodic and lightly arabinosylated repetitive proline-rich proteins (PRPs), through the crosslinked extensins which are periodic and highly arabinosylated, to the arabinogalactan-proteins (AGPs) which are the most highly glycosylated and least periodic. The repetitive units are small, often only four- to six-residue-glycosylated modules viewed hypothetically as functional motifs, or glycomodules. The Hyp contiguity hypothesis predicts that Hyp arabinosylation increases with Hyp contiguity and that clustered noncontiguous Hyp residues are sites of arabinogalactan polysaccharide addition in the AGPs and gums. Recent results involving glycosylation site mapping of endogenous HRGPs and HRGP design using synthetic genes have corroborated the hypothesis. The uses of synthetic genes in HRGP glycosylation site mapping and structural/functional analysis are also discussed.

Key words. Cell wall; hydroxyproline-rich glycoproteins; extensin; arabinogalactan protein; proline-rich protein; O-glycosylation.

Copyright information

© Birkhäuser Verlag, 2001

Authors and Affiliations

  • M.J. Kieliszewski
    • 1
  • E. Shpak
    • 1
  1. 1.Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701 (USA), e-mail: kielisze@helios.phy.ohiou.eduUS