Les include 300 M proteins in 20 mM Na phosphate pH six.five, 2 mM DTT.

Les include 300 M proteins in 20 mM Na phosphate pH six.5, two mM DTT. The spectra had been recorded at 700 MHz and 25 C. (For interpretation from the references to colour within this figure legend, the reader is referred for the web version of this article.)Serena Faggiano et al. / FEBS Open Bio three (2013) 453[11] Komander, D. (2009) The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 93753. [12] Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.W. et al. (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complicated with ubiquitin aldehyde. Cell 111, 1041054. [13] Misaghi, S., Galardy, P.J., Meester, W.J., Ovaa, H., Ploegh, H.L. and Gaudet, R. (2005) Structure on the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. 280, 1512520. [14] Wiener, R., Zhang, X., Wang, T. and Wolberger, C. (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483, 61822. [15] Zheng, N., Schulman, B.A., Song, L., Miller, J.J., Jeffrey, P.D., Wang, P. et al. (2002) Structure in the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complicated. Nature 416, 70309. [16] Kamadurai, H.B., Souphron, J., Scott, D.C., Duda, D.M., Miller, D.J., Stringer, D. et al. (2009) Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex. Mol. Cell 36, 1095102. [17] Maspero, E., Valentini, E., Mari, S., Cecatiello, V., Soffientini, P., Pasqualato, S. et al. (2013) Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming. Nat. Struct. Mol. Biol. 20, 69601. [18] Olsen, S.K. and Lima, C.D. (2013) Structure of a ubiquitin E1-E2 complicated: insights to E1-E2 thioester transfer. Mol. Cell 49, 88496. [19] Hejjaoui, M.BMS-986278 , Haj-Yahya, M.Telmisartan , Kumar, K.S., Brik, A. and Lashuel, H.A. (2011) Towards elucidation in the part of ubiquitination in the pathogenesis of Parkinson’s illness with semisynthetic ubiquitinated alpha-synuclein. Angew. Chem. Int. Ed. Engl. 50, 40509. [20] McGinty, R.K., Kim, J., Chatterjee, C., Roeder, R.G. and Muir, T.W. (2008) Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 453, 81216. [21] Spasser, L. and Brik, A. (2012) Chemistry and biology of your ubiquitin signal. Angew. Chem. Int. Ed. Engl. 51, 6840862. [22] Virdee, S., Ye, Y., Nguyen, D.P., Komander, D. and Chin, J.W. (2010) Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase.PMID:24834360 Nat. Chem. Biol. six, 75057. [23] Virdee, S., Kapadnis, P.B., Elliott, T., Lang, K., Madrzak, J., Nguyen, D.P. et al. (2011) Traceless and site-specific ubiquitination of recombinant proteins. J. Am. Chem. Soc. 133, 107080711. [24] Keren-Kaplan, T., Attali, I., Motamedchaboki, K., Davis, B.A., Tanner, N., Reshef, Y. et al. (2012) Synthetic biology strategy to reconstituting the ubiquitylation cascade in bacteria. EMBO J. 31, 37890. [25] Nicastro, G., Menon, R.P., Masino, L., Knowles, P.P., McDonald, N.Q. and Pastore, A. (2005) The option structure of your Josephin domain of ataxin-3: structural determinants for molecular recognition. Proc. Natl. Acad. Sci. USA 102, 1049310498. [26] Weeks, S.D., Grasty, K.C., Hernandez-Cuebas, L. and Loll, P.J. (2011) Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity. J. Biol. Chem. 286, 4555565. [27] Todi, S.V., Winborn, B.J., Scaglione, K.M., Blount, J.R., Travis, S.M. and Paulson, H.L. (2009.