Literature DB >> 27424748

SUMO Chain Formation by Plant Enzymes.

Konstantin Tomanov1, Ionida Ziba1, Andreas Bachmair2.   

Abstract

SUMO conjugation is a conserved process of eukaryotes, and essential in metazoa. Different isoforms of SUMO are present in eukaryotic genomes. Saccharomyces cerevisiae has only one SUMO protein, humans have four and Arabidopsis thaliana has eight, the main isoforms being SUMO1 and SUMO2 with about 95 % identity. Functionally similar to human SUMO2 and SUMO3, Arabidopsis SUMO1 and 2 can form chains, even though they do not possess a consensus SUMOylation motif. The surprising finding that plants have dedicated enzymes for chain synthesis implies a specific role for SUMO chains in plants. By the cooperative action with SUMO chain recognizing ubiquitin ligases, chains might channel substrates into the ubiquitin-dependent degradation pathway.A method is described to generate SUMO chains, using plant enzymes produced in E. coli. In vitro SUMO chain formation may serve for further analysis of SUMO chain functions. It can also provide an easy-to-synthesize substrate for SUMO-specific proteases.

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Keywords:  Maltose binding protein fusion; Protein expression and purification; SUMO chains; SUMO-specific protease activity; Small ubiquitin-related modifier SUMO

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Year:  2016        PMID: 27424748     DOI: 10.1007/978-1-4939-3759-2_8

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  1 in total

1.  SUMO chain formation relies on the amino-terminal region of SUMO-conjugating enzyme and has dedicated substrates in plants.

Authors:  Konstantin Tomanov; Lilian Nehlin; Ionida Ziba; Andreas Bachmair
Journal:  Biochem J       Date:  2018-01-02       Impact factor: 3.857

  1 in total

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