Extensin: repetitive motifs, functional sites, post‐translational codes, and phylogeny

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Abstract
Homologous hydroxyproline‐rich glycoproteins (HRGPs) of the plant extracellular matrix include extensins, repetitive proline‐rich proteins (RPRPs), some nodulins, gum arabic glycoprotein (GAGP), arabinogalactan‐proteins (AGPs), and chimeric proteins such as potato lectin which contain an extensin module fused to a lectin. The key to the role of HRGPs in cell wall self‐assembly and cell extension lies in their chemistry, which is dependent on extensive post‐translational modifications (PTMs): hydroxylation, glycosylation, and cross‐linking. Repetitive peptide motifs characterize HRGPs. One or more repetitive peptide motifs and their variants, singly or in combination, may constitute functional sites involved in various aspects of cell wall assembly, as follows: Rules for the post‐translational modifications are emerging: Their protistan origin obscures the phylogenetic affinities of a single extensin‐HRGP family due to their sequence divergence. We propose a phylogenetic series ranging from the minimally glycosylated basic RPRPs to the highly glycosylated acidic AGPs. Furthermore, based on similarities between dicots and gymnosperm extensins, and their marked difference from graminaceous monocot extensins, graminaceous monocot and dicot lines may have diverged as early as the progymnosperms. The origin of the embryophytes (land plants) is an even more open question, the nearest extant algal relatives being unknown. The Charophyta, frequently suggested as ancestral to the embryophytes, seem unlikely as the Charalean cell wall of Chara and Nitella lacks hydroxyproline.

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