Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
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.

Bibliography

del Pozo, J. C., & Estelle, M. (1999). The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1. Proceedings of the National Academy of Sciences, 96(26), 15342–15347.

Authors 2
  1. J. C. del Pozo (first)
  2. M. Estelle (additional)
References 27 Referenced 133
  1. P J Davis Plant Hormones Physiology, Biochemistry and Molecular Biology, ed P J Davies (Kluwer, Dordrecht, the Netherlands), pp. 1–12 (1995). (10.1007/978-94-011-0473-9) / Plant Hormones Physiology, Biochemistry and Molecular Biology by Davis P J (1995)
  2. L Walker, M Estelle Curr Opin Plant Biol 1, 434–439 (1998). (10.1016/S1369-5266(98)80269-0) / Curr Opin Plant Biol by Walker L (1998)
  3. J C del Pozo, M Estelle Trends Plant Sci 3, 107–111 (1998). / Trends Plant Sci by del Pozo J C (1998)
  4. M Hochstrasser Genes Dev 12, 901–907 (1998). (10.1101/gad.12.7.901) / Genes Dev by Hochstrasser M (1998)
  5. D Lammer, N Mathias, J M Laplaza, W Jiang, Y Liu, J Callis, M Goebel, M Estelle Genes Dev 12, 914–926 (1998). (10.1101/gad.12.7.914) / Genes Dev by Lammer D (1998)
  6. F Osaka, H Kawasaki, N Aida, M Saeki, T Chiba, S Kawashima, K Tanaka, S Kato Genes Dev 12, 2263–2268 (1998). (10.1101/gad.12.15.2263) / Genes Dev by Osaka F (1998)
  7. D Liakopoulos, T Busgen, A Brychzy, S Jentsch, A Pause Proc Natl Acad Sci USA 96, 5510–5515 (1999). (10.1073/pnas.96.10.5510) / Proc Natl Acad Sci USA by Liakopoulos D (1999)
  8. D Liakopoulos, G Doenges, K Matuschewski, S Jentsch EMBO J 17, 2208–2214 (1998). (10.1093/emboj/17.8.2208) / EMBO J by Liakopoulos D (1998)
  9. J C del Pozo, C Timpte, S Tan, J Callis, M Estelle Science 280, 1760–1763 (1998). (10.1126/science.280.5370.1760) / Science by del Pozo J C (1998)
  10. A Hershko, A Ciechanover Annu Rev Biochem 67, 425–479 (1998). (10.1146/annurev.biochem.67.1.425) / Annu Rev Biochem by Hershko A (1998)
  11. H Wada, E T Yeh, T Kamitani Biochem Biophys Res Commun 257, 100–105 (1999). (10.1006/bbrc.1999.0339) / Biochem Biophys Res Commun by Wada H (1999)
  12. E E Patton, A R Willems, M Tyers Trends Genet 14, 236–243 (1998). (10.1016/S0168-9525(98)01473-5) / Trends Genet by Patton E E (1998)
  13. W M Gray, J C del Pozo, L Walker, L Hobbie, E Risseeuw, T Banks, W L Crosby, M Yang, H Ma, M Estelle Genes Dev 13, 1678–1691 (1999). (10.1101/gad.13.13.1678) / Genes Dev by Gray W M (1999)
  14. M Ruegger, E Dewey, W M Gray, L Hobbie, J Turner, M Estelle Genes Dev 12, 198–207 (1998). (10.1101/gad.12.2.198) / Genes Dev by Ruegger M (1998)
  15. P M Hatfield, R D Vierstra J Biol Chem 267, 14799–14803 (1992). (10.1016/S0021-9258(18)42110-2) / J Biol Chem by Hatfield P M (1992)
  16. M L Sullivan, T B Carpenter, R D Vierstra Plant Mol Biol 24, 651–661 (1994). (10.1007/BF00023561) / Plant Mol Biol by Sullivan M L (1994)
  17. , eds F M Ausubel, R Brent, R E Kingston, D D Moore, J G Seidman, J A Smith, K Struhl (Wiley, New York Current Protocols in Molecular Biology, 1990). / Current Protocols in Molecular Biology by Ausubel F M (1990)
  18. D C Baulcombe, G R Saunders, M W Bevan, M A Mayo, B D Harrison Nature (London) 321, 446–449 (1989). (10.1038/321446a0) / Nature (London) by Baulcombe D C (1989)
  19. N Bechtold, J Ellis, G Pelletier Counc Res Acad Sci Paris Life Sci 316, 15–18 (1993). / Counc Res Acad Sci Paris Life Sci by Bechtold N (1993)
  20. A L Haas, J V Warms, I A Rose Biochemistry 22, 4388–4394 (1983). (10.1021/bi00288a007) / Biochemistry by Haas A L (1983)
  21. S Jentsch, W Seufert, T Sommer, H A Reins Trends Biochem Sci 15, 195–198 (1990). (10.1016/0968-0004(90)90161-4) / Trends Biochem Sci by Jentsch S (1990)
  22. E S Johnson, J I Schwienhorst, R J Dohmen, G Blobel EMBO J 16, 5509–5519 (1997). (10.1093/emboj/16.18.5509) / EMBO J by Johnson E S (1997)
  23. A L Haas, T J Siepmann FASEB J 11, 1257–1268 (1997). (10.1096/fasebj.11.14.9409544) / FASEB J by Haas A L (1997)
  24. A L Haas, J V B Warms, A Hershko, I A Rose J Biol Chem 257, 2543–2548 (1982). (10.1016/S0021-9258(18)34958-5) / J Biol Chem by Haas A L (1982)
  25. M J Matunis, E Coutavas, G Blobel J Cell Biol 135, 1457–1470 (1996). (10.1083/jcb.135.6.1457) / J Cell Biol by Matunis M J (1996)
  26. S Müller, M J Matunis, A Dejean EMBO J 17, 61–70 (1998). (10.1093/emboj/17.1.61) / EMBO J by Müller S (1998)
  27. J M Desterro, M S Rodrigez, R T Hay Mol Cell 2, 233–239 (1998). (10.1016/S1097-2765(00)80133-1) / Mol Cell by Desterro J M (1998)
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)
Funders 0

None

@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} }