Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1996 Jan 23;93(2):856–860. doi: 10.1073/pnas.93.2.856

Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome.

S van Nocker 1, Q Deveraux 1, M Rechsteiner 1, R D Vierstra 1
PMCID: PMC40147  PMID: 8570648

Abstract

Multiubiquitin chain attachment is a key step leading to the selective degradation of abnormal polypeptides and many important regulatory proteins by the eukaryotic 26S proteasome. However, the mechanism by which the 26S complex recognizes this posttranslational modification is unknown. Using synthetic multiubiquitin chains to probe an expression library for interacting proteins, we have isolated an Arabidopsis cDNA, designated MBP1, that encodes a 41-kDa acidic protein exhibiting high affinity for chains, especially those containing four or more ubiquitins. Based on similar physical and immunological properties, multiubiquitin binding affinities, and peptide sequence, MBP1 is homologous to subunit 5a of the human 26S proteasome. Structurally related proteins also exist in yeast, Caenorhabditis, and other plant species. Given their binding properties, association with the 26S proteasome, and widespread distribution, MBP1, S5a, and related proteins likely function as essential ubiquitin recognition components of the 26S proteasome.

Full text

PDF
856

Images in this article

858Fig. 1
on p.858
859Fig. 2
on p.859
859Fig. 3
on p.859
859Fig. 4
on p.859

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arnason T., Ellison M. J. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol Cell Biol. 1994 Dec;14(12):7876–7883. doi: 10.1128/mcb.14.12.7876. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beal R., Deveraux Q., Xia G., Rechsteiner M., Pickart C. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):861–866. doi: 10.1073/pnas.93.2.861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chau V., Tobias J. W., Bachmair A., Marriott D., Ecker D. J., Gonda D. K., Varshavsky A. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science. 1989 Mar 24;243(4898):1576–1583. doi: 10.1126/science.2538923. [DOI] [PubMed] [Google Scholar]
  4. Chen Z., Pickart C. M. A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin. J Biol Chem. 1990 Dec 15;265(35):21835–21842. [PubMed] [Google Scholar]
  5. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell. 1994 Oct 7;79(1):13–21. doi: 10.1016/0092-8674(94)90396-4. [DOI] [PubMed] [Google Scholar]
  6. Dean C., Tamaki S., Dunsmuir P., Favreau M., Katayama C., Dooner H., Bedbrook J. mRNA transcripts of several plant genes are polyadenylated at multiple sites in vivo. Nucleic Acids Res. 1986 Mar 11;14(5):2229–2240. doi: 10.1093/nar/14.5.2229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Deveraux Q., Ustrell V., Pickart C., Rechsteiner M. A 26 S protease subunit that binds ubiquitin conjugates. J Biol Chem. 1994 Mar 11;269(10):7059–7061. [PubMed] [Google Scholar]
  8. Deveraux Q., van Nocker S., Mahaffey D., Vierstra R., Rechsteiner M. Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a. J Biol Chem. 1995 Dec 15;270(50):29660–29663. doi: 10.1074/jbc.270.50.29660. [DOI] [PubMed] [Google Scholar]
  9. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fujinami K., Tanahashi N., Tanaka K., Ichihara A., Cejka Z., Baumeister W., Miyawaki M., Sato T., Nakagawa H. Purification and characterization of the 26 S proteasome from spinach leaves. J Biol Chem. 1994 Oct 14;269(41):25905–25910. [PubMed] [Google Scholar]
  11. Glotzer M., Murray A. W., Kirschner M. W. Cyclin is degraded by the ubiquitin pathway. Nature. 1991 Jan 10;349(6305):132–138. doi: 10.1038/349132a0. [DOI] [PubMed] [Google Scholar]
  12. Gregori L., Poosch M. S., Cousins G., Chau V. A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis. J Biol Chem. 1990 May 25;265(15):8354–8357. [PubMed] [Google Scholar]
  13. Haracska L., Udvardy A. Cloning and sequencing a non-ATPase subunit of the regulatory complex of the Drosophila 26S protease. Eur J Biochem. 1995 Aug 1;231(3):720–725. doi: 10.1111/j.1432-1033.1995.tb20753.x. [DOI] [PubMed] [Google Scholar]
  14. Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu Rev Biochem. 1992;61:761–807. doi: 10.1146/annurev.bi.61.070192.003553. [DOI] [PubMed] [Google Scholar]
  15. Hochstrasser M., Ellison M. J., Chau V., Varshavsky A. The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4606–4610. doi: 10.1073/pnas.88.11.4606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hough R., Pratt G., Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J Biol Chem. 1987 Jun 15;262(17):8303–8313. [PubMed] [Google Scholar]
  17. Jabben M., Shanklin J., Vierstra R. D. Ubiquitin-phytochrome conjugates. Pool dynamics during in vivo phytochrome degradation. J Biol Chem. 1989 Mar 25;264(9):4998–5005. [PubMed] [Google Scholar]
  18. Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S. Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science. 1994 Sep 30;265(5181):2077–2082. doi: 10.1126/science.8091229. [DOI] [PubMed] [Google Scholar]
  19. Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science. 1995 Apr 28;268(5210):533–539. doi: 10.1126/science.7725097. [DOI] [PubMed] [Google Scholar]
  20. Madura K., Varshavsky A. Degradation of G alpha by the N-end rule pathway. Science. 1994 Sep 2;265(5177):1454–1458. doi: 10.1126/science.8073290. [DOI] [PubMed] [Google Scholar]
  21. Palombella V. J., Rando O. J., Goldberg A. L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell. 1994 Sep 9;78(5):773–785. doi: 10.1016/s0092-8674(94)90482-0. [DOI] [PubMed] [Google Scholar]
  22. Peters J. M. Proteasomes: protein degradation machines of the cell. Trends Biochem Sci. 1994 Sep;19(9):377–382. doi: 10.1016/0968-0004(94)90115-5. [DOI] [PubMed] [Google Scholar]
  23. Rechsteiner M., Hoffman L., Dubiel W. The multicatalytic and 26 S proteases. J Biol Chem. 1993 Mar 25;268(9):6065–6068. [PubMed] [Google Scholar]
  24. Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A. L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 1994 Sep 9;78(5):761–771. doi: 10.1016/s0092-8674(94)90462-6. [DOI] [PubMed] [Google Scholar]
  25. Rosenberg A. H., Lade B. N., Chui D. S., Lin S. W., Dunn J. J., Studier F. W. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene. 1987;56(1):125–135. doi: 10.1016/0378-1119(87)90165-x. [DOI] [PubMed] [Google Scholar]
  26. Scheffner M., Huibregtse J. M., Vierstra R. D., Howley P. M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell. 1993 Nov 5;75(3):495–505. doi: 10.1016/0092-8674(93)90384-3. [DOI] [PubMed] [Google Scholar]
  27. Spence J., Sadis S., Haas A. L., Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol. 1995 Mar;15(3):1265–1273. doi: 10.1128/mcb.15.3.1265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Sudo K., Chinen K., Nakamura Y. 2058 expressed sequence tags (ESTs) from a human fetal lung cDNA library. Genomics. 1994 Nov 15;24(2):276–279. doi: 10.1006/geno.1994.1616. [DOI] [PubMed] [Google Scholar]
  29. Treier M., Staszewski L. M., Bohmann D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell. 1994 Sep 9;78(5):787–798. doi: 10.1016/s0092-8674(94)90502-9. [DOI] [PubMed] [Google Scholar]
  30. Van De Loo F. J., Turner S., Somerville C. Expressed Sequence Tags from Developing Castor Seeds. Plant Physiol. 1995 Jul;108(3):1141–1150. doi: 10.1104/pp.108.3.1141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Van Nocker S., Vierstra R. D. Cloning and characterization of a 20-kDa ubiquitin carrier protein from wheat that catalyzes multiubiquitin chain formation in vitro. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10297–10301. doi: 10.1073/pnas.88.22.10297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  33. van Nocker S., Vierstra R. D. Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway. J Biol Chem. 1993 Nov 25;268(33):24766–24773. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES