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Published on January 16, 2009; 10.1104/pp.108.135053

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Received December 29, 2008
Accepted January 10, 2009

Substrates Related to Chromatin and to RNA-Dependent Processes Are Modified by Arabidopsis SUMO Isoforms that Differ in a Conserved Residue with Influence on De-Sumoylation

Ruchika Budhiraja , Rebecca Hermkes , Stefan Muller , Jurgen Schmidt , Thomas Colby , Kishore Panigrahi , George Coupland , and Andreas Bachmair *

Dept. of Plant Developmental Biology and Mass Spectrometry Group, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, D-50829 Cologne, Germany; Inst. of Biochemistry, Univ. of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany; Dept. of Biochemistry, Max F. Perutz Laboratories, Univ. of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna Austria

* Corresponding author; email: andreas.bachmair{at}univie.ac.at.

The higher plant Arabidopsis thaliana has eight genes potentially coding for small ubiquitin-related modifier (SUMO) proteins. However, two well-expressed isoforms differ from fungal and animal consensus in a conserved Gln residue situated four residues from the carboxyl terminus. We tested deviations in this position in the background of SUMO1, the isoform with the highest expression level, and found that changes do not prevent conjugation to substrate proteins in vivo. Replacement of this conserved Gln by Ala resulted in a protein that was less readily removed from a substrate by SUMO protease ESD4 in an in vitro reaction, and apparently led to higher levels of SUMO conjugates when expressed in vivo. We used SUMO1 variant with Gln to Ala substitution, as well as SUMO3 and SUMO5 (which carry Met and Leu, respectively, at this position) to enrich in vivo substrates. Identification of the most abundant proteins contained in these fractions indicated that they are involved in DNA-related, or in RNA-dependent processes, such as regulation of chromatin structure, splicing, or translation. The majority of the identified bona fide substrates contain predicted sumoylation sites. A subset of the proteins was expressed in E. coli and could be sumoylated in vitro.




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S. Okada, M. Nagabuchi, Y. Takamura, T. Nakagawa, K. Shinmyozu, J.-i. Nakayama, and K. Tanaka
Reconstitution of Arabidopsis thaliana SUMO Pathways in E. coli: Functional Evaluation of SUMO Machinery Proteins and Mapping of SUMOylation Sites by Mass Spectrometry
Plant Cell Physiol., June 1, 2009; 50(6): 1049 - 1061.
[Abstract] [Full Text] [PDF]


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