E3-independent ubiquitination of AtMAPR/MSBP1

AtMAPR5/MSBP1 and its homologs can be ubiquitinated in the absence of E3 ligase in in vitro ubiquitination assays. Ubiquitinated AtMAPR3 and AtMAPR5/MSBP1 were identified using LC–MS/MS. Representative MS/MS spectra showing the signature peptide Gly–Gly tag on Lys residue of ubiquitinated-AtMAPR3. [...

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Veröffentlicht in:	Phytochemistry (Oxford) 2012-06, Vol.78, p.7-19
Hauptverfasser:	Kao, Ai-Ling, Lin, Ying-Han, Chen, Rita P.-Y., Huang, Yun-Yen, Chen, Ching-Chung, Yang, Chien-Chih
Format:	Artikel
Sprache:	eng
Schlagworte:	Arabidopsis - enzymology Arabidopsis - metabolism Arabidopsis Proteins - metabolism Arabidopsis thaliana Carrier Proteins - metabolism Cruciferae Electrophoresis, Polyacrylamide Gel Humans Ubiquitin binding domain Ubiquitin-Protein Ligases - metabolism Ubiquitination Ubiquitination - physiology
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