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Coimmunoprecipitation of reversibly glycosylated polypeptide with sucrose synthase from developing castor oilseeds
Author(s) -
Fedosejevs Eric T.,
Liu Leo N.C.,
Abergel Megan,
She YiMin,
Plaxton William C.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12893
Subject(s) - chemistry , ricinus , immunoprecipitation , western blot , blot , glycoprotein , biochemistry , glycolipid , sucrose synthase , sucrose , invertase , gene
The sucrose synthase ( SUS ) interactome of developing castor oilseeds ( COS ; Ricinus communis ) was assessed using coimmunoprecipitation (co‐ IP ) with anti‐( COS Rc SUS 1)‐IgG followed by proteomic analysis. A 41‐ kD a polypeptide (p41) that coimmunoprecipitated with Rc SUS 1 from COS extracts was identified as reversibly glycosylated polypeptide‐1 (Rc RGP 1) by LC ‐ MS / MS and anti‐Rc RGP 1 immunoblotting. Reciprocal Far‐western immunodot blotting corroborated the specific interaction between Rc SUS 1 and Rc RGP 1. Co‐ IP using anti‐( COS Rc SUS 1)‐IgG and clarified extracts from other developing seeds as well as cluster (proteoid) roots of white lupin and Harsh Hakea consistently recovered 90 kD a SUS polypeptides along with p41/ RGP as a SUS interactor. The results suggest that SUS interacts with RGP in diverse sink tissues to channel UDP ‐glucose derived from imported sucrose into hemicellulose and/or glycoprotein/glycolipid biosynthesis.