Ubiquitin biochemistry

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Schneider D M, Deliwo M J and Wand A J 1992 Fast internal main-chain dynamics of human ubiquitin Biochemistry 31 3645-52... 

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The reader should consult earlier reviews [70, 94, 95] and other chapters in this volume for a detailed discussion of UbL biology and biochemistry. There are two important points for the current discussion. First, the conjugation cascades of UbLs differ from that of ubiquitin chiefly in terms of complexity - there is one conjugating enzyme per UbL, and many fewer E3s. Second, because modifier proteins (including ubiquitin) do not interact strongly with their dedicated E2s (Section 5.6.1), it is believed that El enzymes play the major role in matching E2s with the correct modifier protein (see Ref [96]). 

Cook, W. J., Jeffrey, L. C., Xu, Y., and Chau, V. Tertiary structures of class 1 ubiquitin-conjugating enzymes are highly conserved crystal structure of yeast Ubc4. Biochemistry 1993, 32, 13809-17. 

Beeleth, E. S. and Pickart, C. M. Mechanism of ubiquitin conjugating enzyme E2—230K catalysis involving a thiol relay Biochemistry 1995, 35, 1664-71. 

SCHLESINGER, D. H., GOLDSTEIN, G., and Niall, H. D. The complete amino add sequence of ubiquitin, an adenylate cydase stimulating polypeptide probably universal in living cells, Biochemistry, 1975, 14, 2214-8. 

Larsen, C. N., Krantz, B. A., and Wilkinson, K. D. Substrate specificity of deubiquitinating enzymes ubiquitin C-terminal hydrolases. Biochemistry, 1998, 37, 3358-68. 

Dang, L. C., Melandri, F. D., and Stein, R. L. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry, 1998, 37, 1868—79. 

K. D. Nonhydrolyzable diubiquitin analogues are inhibitors of ubiquitin conjugation and deconjugation. Biochemistry, 2000, 39, 10001-10. 

Sakamoto, T., Tanaka, T., Ito, Y., et al. (1999) An NMR analysis of ubiquitin recognition by yeast ubiquitin hydrolase evidence for novel substrate recognitionby a cysteine protease. Biochemistry 38, 11,634-11,642. 

Rajesh, S., Sakamoto, T., Iwamoto-Sugai, M., Shibata, T., Kohno, T., and Ito, Y. (1999) Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation. Biochemistry 38, 9242-9253. 

Mizutani A, Nakagawa N, Hitomi K, and Tsukagoshi N (1997) Ascorbate-dependent expression of ubiquitin genes in guinea pigs. International Journal of Biochemistry and... 

Krantz, B.A. Sosnick, T.R. Distinguishing between two-state and three-state models for ubiquitin folding. Biochemistry 2000, 39, 11696-11701. 

Marotti, L.A., R. Newitt, Y. Wang, R. Aebersold and H.G. Dohlman. Direct identification of a G protein ubiquitination site by mass spectrometry. Biochemistry 41 5067-5074, 2002. 

Klemperer, N.S., E.S. Berleth and C.M. Pickart. A novel, arsenite-sensitive E2 of the ubiquitin pathway purification and properties. Biochemistry 28 6035-6041, 1989. 

Yeung, S.J., Chen, S.H., Chan, L. 1996. Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B. Biochemistry 35 13843-13848. 

Tolbert, B.S., Tajc, S.G., Webb, H., Snyder, J., Nielsen, J.E., Miller, B.L., Basavappa, R. The active site cysteine of ubiquitin-conjugating enzymes has a significantly elevated pK(a) Functional implications. Biochemistry 2005, 44,16385-91. 

Pan, J.X., Wilson, D.J., Konermann, L. (2005) Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments Imphcations for ubiquitin folding. Biochemistry, 44 (24), 8627-8633. 

Hoerner, J.K., Xiao, H., Kaltashov, I.A. (2005) Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry. Biochemistry, 44,11286-11294. 

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