Biochemical and Structural Characterization of the Ubiquitin-Conjugating Enzyme UBE2W Reveals the Formation of a Noncovalent Homodimer

Cell Biochemistry and Biophysics

Volumn 67, Issue 1, 2013, Pages 103-110

  Vittal, Vinayak ^a   Wenzel, Dawn M ^a,b   Brzovic, Peter S ^a   Klevit, Rachel E ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

Dimerization; NMR; UBE2W; Ubiquitin; Ubiquitin conjugating enzyme

Indexed keywords

RECOMBINANT PROTEIN; UBE2W PROTEIN, HUMAN; UBIQUITIN CONJUGATING ENZYME;

ARTICLE; BIOSYNTHESIS; CHEMISTRY; DIMERIZATION; ENZYME ACTIVE SITE; GENETICS; HUMAN; METABOLISM; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE;

CATALYTIC DOMAIN; DIMERIZATION; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; UBIQUITIN-CONJUGATING ENZYMES;

EID: 84883447618     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-013-9633-5     Document Type: Article

References (29)

1. Pickart, C. M. (2001). Mechanisms underlying ubiquitination. Annual Review of Biochemistry, 2001(70), 195-201.
2. Ye, Y., & Rape, M. (2009). Building ubiquitin chains: E2 enzymes at work. Nature Reviews Molecular Cell Biology, 10, 755-764.
3. Christensen, D. E., Brzovic, P. S., & Klevit, R. E. (2007). E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages. Nature Structural and Molecular Biology, 14, 941-948.
4. Rodrigo-Brenni, M. C., Foster, S. A., & Morgan, D. O. (2010). Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin. Molecular Cell, 39, 548-559.
5. Alpi, A. F., Pace, P. E., Babu, M. M., & Patel, K. J. (2008). Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI. Molecular Cell, 32, 767-777.
6. Scaglione, K. M., Zavodszky, E., Todi, S. V., Patury, S., Xu, P., Rodríguez-Lebrón, E., et al. (2011). Ube2w and Ataxin-3 Coordinately Regulate the Ubiquitin Ligase CHIP. Molecular Cell, 43, 599-612.
7. Pickart, C. M., & Raasi, S. (2005). Controlled synthesis of polyubiquitin chains. Methods in Enyzmology, 399, 21-36.
8. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995). NMRPipe: A multidimensional spectral processing system based on UNIX pipes. Journal of Biomolecular NMR, 6, 277-293.
9. Johnson, B. A., & Blevins, R. A. (1994). NMR view: A computer program for the visualization and analysis of NMR data. Journal of Biomolecular NMR, 4, 603-614.
10. Kelley, L. A., & Sternberg, M. J. E. (2009). Protein structure prediction on the web: A case study using the Phyre server. Nature Protocols, 4, 363-371.
11. Juan, Y. C., Landry, M. C., Sanches, M., Vittal, V., Leung, C. C., Ceccarelli, D. F., et al. (2012). OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function. Molecular Cell, 45, 384-397.
12. Sheng, Y., Hong, J. H., Doherty, R., Srikumar, T., Shloush, J., Avvakumov, G. V., et al. (2012). A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Molecular Cell Proteomics. 2012. 11, 329-341.
13. Brzovic, P. S., Lissounov, A., Christensen, D. E., Hoyt, D. W., & Klevit, R. E. (2006). A UbcH5c/ubiquitin noncovalent complex is required for processive BRCA1-direct ubiquitination. Molecular Cell, 21, 873-880.
14. Sakata, E., Satoh, T., Yamamoto, S., Yamaguchi, Y., Yagi-Utsumi, M., Tanaka, K., et al. (2010). (2010) Crystal structure of UbcH5b ~ ubiquitin intermediate: Insight into the formation of the self-assembled E2 ~ Ub conjugates. Structure, 18, 138-147.
15. Page, R. C., Pruneda, J. N., Amick, J., Klevit, R. E., & Misra, S. (2012). Structural insights into the conformation and oligomerization of E2 ~ ubiquitin conjugates. Biochemistry, 51, 4175-4187.
16. Das, R., Mariano, J., Tsai, Y. C., Kalathur, R. C., Kostova, Z., Li, J., et al. (2009). Allosteric activation of E2-RING finger-mediate ubiquityation by a structurally defined specific E2-binding region of gp78. Molecular Cell, 34, 674-685.
17. Li, W., Tu, D., Li, L., Wollert, T., Ghirlando, R., Brunger, et al. (2009). Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proceedings of the National Academy of Sciences of the United States of America. 106, 3722-3727.
18. Hibbert, R. G., Huang, A., Boelens, R., & Sixma, T. K. (2011). E3 ligase Rad18 promotes monubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America, 108, 5590-5595.
19. VanDermark, A. P., Hofmann, R. M., Tsui, C., Pickart, C. M., & Wolberger, C. (2001). Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer. Cell, 105, 711-720.
20. Moraes, T. F., Edwards, R. A., McKenna, S., Pastushok, L., Xiao, W., Glover, J. N., et al. (2001). Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Natural Structural Biology, 8, 669-673.
21. Pickart, C. E., & Rose, I. A. (1985). Functional heterogeneity of ubiquitin carrier proteins. Journal of Biological Chemistry, 260, 1573-1581.
22. Silver, E. T., Gwozd, T. J., Ptak, C., Goebl, M., & Ellison, M. J. (1992). A chimeric ubiquitin conjugating enzyme that combins the cell cycle properties of CDC34 (UBC3) and the DNA repair properties of RAD6 (UBC2): Implications for the structure, function and evolution of the E2s. EMBO Journal, 11, 3091-3098.
23. Girod, P. A., & Vierstra, R. D. (1993). A major ubiquitin conjugation system in wheat germ extracts involves a 15-kDa ubiquitin-conjugating enzyme (E2) homologous to the years UBC4/UBC5 gene products. Journal of Biological Chemistry, 268, 955-960.
24. Ptak, C., Prendergast, J. A., Hodgins, R., Kay, C. M., Chau, V., & Ellison, M. J. (1994). Functional and physical characterization of the cell cycle ubiquitin-conjugating enzyme CDC34 (UBC3). Identification of a functional determinant within the tail that facilitates CDC34 self-association. Journal of Biological Chemistry, 269, 26539-26545.
25. Haldeman, M. T., Xia, G., Kasperek, E. M., & Pickart, C. M. (1997). Structure and function of ubiquitin conjugating enzyme E2-25K: The tail is a core-dependent activity element. Biochemistry, 36, 10526-10537.
26. Gazdoiu, S., Yamoah, K., Wu, K., Escalante, C. R., Tappin, I., Bermudez, V., et al. (2005). Proximity-induced activation of human Cdc34 through heterologous dimerization. Proceedings of the National Academy of Sciences of the United States of America, 102(2005), 15053-15058.
27. Varelas, X., Ptak, C., & Ellison, M. J. (2003). Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity. Molecular and Cellular Biology, 23, 5388-5400.
28. Skowyra, D., Graig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell, 91, 209-219.
29. Deffenbaugh, A. E., Scaglione, K. M., Zhang, L., Moore, J. M., Buranda, T., Sklar, L. A., et al. (2003). Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1. Cell, 114, 611-622.