Abstract
The ubiquitin-like protein RUB1 is conjugated to target proteins by a mechanism similar to that of ubiquitin conjugation. Genetic studies in Arabidopsis thaliana have implicated the RUB-conjugation pathway in auxin response. The first step in the pathway is RUB activation by a bipartite enzyme composed of the AXR1 and ECR1 proteins. Ubiquitin activation is an ATP-dependent process that involves the formation of an AMP-ubiquitin intermediate. Here we show that RUB activation by AXR1-ECR1 also involves formation of an AMP-RUB intermediate and that this reaction is catalyzed by the ECR1 subunit alone. In addition, we identified an Arabidopsis protein called RCE1 that is a likely RUB-conjugating enzyme. RCE1 works together with AXR1-ECR1 to promote formation of a stable RUB conjugate with the Arabidopsis cullin AtCUL1 in vitro . Using a tagged version of RUB1, we show that this modification occurs in vivo . Because AtCUL1 is a component of the ubiquitin protein ligase SCF TIR1 , a complex that also functions in auxin response, we propose that RUB modification of AtCUL1 is important for auxin response.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:31 a.m.) |
Deposited | 3 years, 2 months ago (June 7, 2022, 12:25 a.m.) |
Indexed | 3 weeks, 3 days ago (Aug. 5, 2025, 8:48 a.m.) |
Issued | 25 years, 8 months ago (Dec. 21, 1999) |
Published | 25 years, 8 months ago (Dec. 21, 1999) |
Published Online | 25 years, 8 months ago (Dec. 21, 1999) |
Published Print | 25 years, 8 months ago (Dec. 21, 1999) |
@article{del_Pozo_1999, title={The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.26.15342}, DOI={10.1073/pnas.96.26.15342}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={del Pozo, J. C. and Estelle, M.}, year={1999}, month=dec, pages={15342–15347} }