title: The SUMO conjugation pathway in Populus: genomic analysis, tissue-specific and inducible SUMOylation and in vitro de-SUMOylation.
abstract: Covalent attachment of the small ubiquitin-like modifier (SUMO) to proteins in eukaryotic cells can regulate an assortment of cellular processes including transcription, and DNA-protein and protein-protein interactions. We identified gene models and found evidence for expression of genes involved in SUMOylation and SUMO deconjugation in Populus. We detected SUMOylated proteins in diverse organ and tissue types. SUMOylation was altered during responses to heat shock, desiccation, peroxide and irrigation of roots with high salt solution. SUMO deconjugation from substrates was sensitive to cysteine protease inhibitors. Product sizes and sensitivity to inhibitors are consistent with poly-SUMO chain formation as an intermediate step in SUMO redistribution to substrates in plant cells responding to treatments. The SUMOylation pathway is active in Populus and substrate conjugation to SUMO is a rapid response to multiple inducers.
authors.affiliation: Roskamp Institute, Sarasota, FL 34243, USA.
authors.forename: Jon M
authors.initials: JM
authors.lastname: Reed
authors.forename: Christopher
authors.initials: C
authors.lastname: Dervinis
authors.forename: Alison M
authors.initials: AM
authors.lastname: Morse
authors.forename: John M
authors.initials: JM
authors.lastname: Davis
mesh_terms: D015153:Blotting, Western; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D018745:Genome, Plant; D032107:Populus / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D014452:Ubiquitins / Q000378:metabolism*
chemical_list: D015853:Cysteine Proteinase Inhibitors; C403233:SUMO protein, plant; D014452:Ubiquitins