Characterization of the C-terminal diglycine motif of SUMO-1/3.

Koji Yamada, Miyuki Muramatsu, Daiki Saito, Mai Sato-Oka, Masayuki Saito, Taishi Moriyama, Hisato Saitoh

Journal: Bioscience, biotechnology, and biochemistry 2012;76(5):1035-7

PMID: 22738983

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Abstract

A hallmark of small ubiquitin-related modifier (SUMO) is the production of a C-terminal tail containing diglycines (GGs), which are believed to be required for SUMOylation. Whether GGs are required components in SUMOylation remains unanswered experimentally. In this study we found that the SUMO-1/3-AA/-GS/-GN/-GA mutant can form sodium dodecyl sulfate (SDS)-dithiothreitol (DTT)-resistant complexes with cellular proteins, indicating that the GG motif is not strictly required for SUMOylation.

Address: Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University, Japan.

DOI: 10.1271/bbb.120019

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MeSH Terms: Amino Acid Motifs, Dithiothreitol, Gene Expression, Glycylglycine, Green Fluorescent Proteins, HeLa Cells, Humans, Mutant Chimeric Proteins, Plasmids, Protein Binding, SUMO-1 Protein, Sodium Dodecyl Sulfate, Sumoylation, Transfection, Ubiquitins