Biological significance of structural differences between two highly conserved Ubc variants

Biochemical and Biophysical Research Communications

Volumn 378, Issue 3, 2009, Pages 563-568

  Pelzer, Lindsay ^a   Pastushok, Landon ^a   Moraes, Trevor ^b   Mark Glover, J N ^b   Ellison, Michael J ^b   Ziola, Barry ^a   Xiao, Wei ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Crystal structure; Epitope; Mms2; Monoclonal antibody; Ubiquitination; Uev1

Indexed keywords

AMINO ACID; HETERODIMER; MONOCLONAL ANTIBODY; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME VARIANT 1; UBIQUITIN CONJUGATING ENZYME VARIANT MMS1; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; EPITOPE MAPPING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; CONSERVED SEQUENCE; DIMERIZATION; EPITOPE MAPPING; HUMANS; LIGASES; MICE; MICE, INBRED BALB C; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE DELETION; TRANSCRIPTION FACTORS; UBIQUITIN-CONJUGATING ENZYMES;

EID: 57749206639     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.11.089     Document Type: Article

References (21)

1. Hershko A., and Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67 (1998) 425-479
2. Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., and Chen Z.J. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103 (2000) 351-361
3. Hofmann R.M., and Pickart C.M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96 (1999) 645-653
4. McKenna S., Spyracopoulos L., Moraes T., Pastushok L., Ptak C., Xiao W., and Ellison M.J. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. J. Biol. Chem. 276 (2001) 40120-40126
5. Broomfield S., Chow B.L., and Xiao W. MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway. Proc. Natl. Acad. Sci. USA 95 (1998) 5678-5683
6. McKenna S., Moraes T., Pastushok L., Ptak C., Xiao W., Spyracopoulos L., and Ellison M.J. An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis. J. Biol. Chem. 278 (2003) 13151-13158
7. Pastushok L., Moraes T.F., Ellison M.J., and Xiao W. A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex. J. Biol. Chem. 280 (2005) 17891-17900
8. Moraes T.F., Edwards R.A., McKenna S., Pastushok L., Xiao W., Glover J.N., and Ellison M.J. Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Nat. Struct. Biol. 8 (2001) 669-673
9. VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., and Wolberger C. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 105 (2001) 711-720
10. Xiao W., Lin S.L., Broomfield S., Chow B.L., and Wei Y.F. The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family. Nucleic Acids Res. 26 (1998) 3908-3914
11. Andersen P.L., Zhou H., Pastushok L., Moraes T., McKenna S., Ziola B., Ellison M.J., Dixit V.M., and Xiao W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. J. Cell Biol. 170 (2005) 745-755
12. Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 135-141
13. Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M., Xiao W., and Dixit V.M. Bcl10 activates the NF-κB pathway through ubiquitination of NEMO. Nature 427 (2004) 167-171
14. Lin A., and Karin M. NF-κB in cancer: a marked target. Semin. Cancer Biol. 13 (2003) 107-114
15. Ziola B., Gares S.L., Lorrain B., Gee L., Ingledew W.M., and Lee S.Y. Epitope mapping of monoclonal antibodies specific for the directly cross-linked mesodiaminopimelic acid peptidoglycan found in the anaerobic beer spoilage bacterium Pectinatus cerevisiiphilus. Can. J. Microbiol. 45 (1999) 779-785
16. Gares S.L., Whiting M.S., Ingledew W.M., and Ziola B. Detection and identification of Pectinatus cerevisiiphilus using surface-reactive monoclonal antibodies in a membrane filter-based immunoassay. J. Am. Soc. Brew. Chem. 51 (1993) 158-163
17. Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70 (2001) 503-533
18. Pastushok L., Spyracopoulos L., and Xiao W. Two Mms2 residues cooperatively interact with ubiquitin and are critical for Lys63 polyubiquitination in vitro and in vivo. FEBS Lett. 581 (2007) 5343-5348
19. Li Z., Xiao W., McCormick J.J., and Maher V.M. Identification of a protein essential for a major pathway used by human cells to avoid UV-induced DNA damage. Proc. Natl. Acad. Sci. USA 99 (2002) 4459-4464
20. Syed N.A., Andersen P.L., Warrington R.C., and Xiao W. Uev1A, A ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-κB activation. Apoptosis 11 (2006) 2147-2157
21. Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47 (1991) 110-119