Abstract
Much has been learned about protein ubiquitination by studying the structural, biochemical, and biophysical properties of ubiquitin chains in vitro. However, these analyses were limited to K48-, K63-linked, and linear ubiquitin chains. Only recently, enzymatic and chemical assembly systems for the remaining chain types have been developed. Here, we describe a method to synthesise K11-linked ubiquitin chains in vitro by exploiting the intrinsic K11-specificity of the E2 enzyme UBE2S.
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Bremm, A., Komander, D. (2012). Synthesis and Analysis of K11-Linked Ubiquitin Chains. In: Dohmen, R., Scheffner, M. (eds) Ubiquitin Family Modifiers and the Proteasome. Methods in Molecular Biology, vol 832. Humana Press. https://doi.org/10.1007/978-1-61779-474-2_15
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DOI: https://doi.org/10.1007/978-1-61779-474-2_15
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Publisher Name: Humana Press
Print ISBN: 978-1-61779-473-5
Online ISBN: 978-1-61779-474-2
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