Identification of Proteins Interacting with Ubiquitin Chains

Zhao, Xiaohui; Lutz, Joachim; Höllmüller, Eva; Scheffner, Martin; Marx, Andreas; Stengel, Florian

doi:10.1002/anie.201705898

Cited by 44 publications

(60 citation statements)

References 55 publications

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“…Click reactions with the double mutant of UB generated UB chains of defined linkages through a triazole linker (Eger et al, 2010;Schneider et al, 2014;Rösner et al, 2015). These chains have been used as affinity reagents to identify UBD binding to various chain types (Zhao et al, 2017). UAA p-azidophenylalanine (AzF) has also been used to replace specific Lys sidechains on UB to generate diUB of defined linkages by click chemistry (Fig.…”

Section: Ubiquitin Chain Synthesis Enabled By Unnaturalmentioning

confidence: 99%

Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond

et al. 2020

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Section: Ubiquitin Chain Synthesis Enabled By Unnaturalmentioning

confidence: 99%

Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond

et al. 2020

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“…Firstly, we synthesised the artificially linked

Ub \binom{48}{2 - PA}

dimer based on a previously described approach . Briefly, we bacterially expressed the monomeric C48Ub mutant (replacement of Lys48 by Cys) and, upon purification, functionalised it with an alkyne group through a Michael reaction with PA (C48Ub‐PA; Figures A and S2).…”

Section: Figurementioning

confidence: 99%

Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy

Zhao¹,

Mißun²,

Schneider³

et al. 2019

ChemBioChem

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As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. A facile, click chemistry based approach for the efficient generation of linkage‐defined Ub chains, including Ub dimers, was recently established. Within these chains, individual Ub moieties are connected through a triazole linkage, rather than the natural isopeptide bond. Herein, it is reported that the conformation of an artificially K48‐linked Ub dimer resembles that of the natively linked dimer, with respect to structural and dynamic characteristics, as demonstrated by means of high‐resolution NMR spectroscopy. Thus, it is proposed that artificially linked Ub dimers, as generated by this approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains.

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“…4d) give rise to larger poly-Ub analogues including the biochemical unavailable K27-linked Ub chains. Such stable poly-Ub chains can be employed to study the interacting proteins or 'readers' of the Ub code by performing pull-down experiments and subsequent proteomic analysis using mass spectrometry approaches (Zhao et al 2017;Zhang et al 2017). Fig.…”

Section: (Poly)ub Chainsmentioning

confidence: 99%

How to Target Viral and Bacterial Effector Proteins Interfering with Ubiquitin Signaling

Noort

Ovaa

2018

Current Topics in Microbiology and Immunology

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Ubiquitination is a frequently occurring and very diverse posttranslational modification influencing a wide scope of cellular processes. Ubiquitin (Ub) has the unique ability to form eight different lysine-linked polymeric chains, mixed chains and engages with ubiquitin-like (Ubl) molecules. The distinct signals evoked by specific enzymes play a crucial role in, for instance, proteasome-mediated protein degradation, cell cycle regulation, and DNA damage responses. Due to the large variety of cellular functions that this posttranslational modification influences, the enzymes that construct such Ub modifications, and subsequently controle and degrade these signals, is enormous. In this chapter, we will discuss the current state-of-the-art of activity-based probes, reporter substrates, and other relevant tools based on Ub as recognition element, to study the enzymes involved in the complex system of ubiquitination.

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Identification of Proteins Interacting with Ubiquitin Chains

Cited by 44 publications

References 55 publications

Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond

Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond

Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy

How to Target Viral and Bacterial Effector Proteins Interfering with Ubiquitin Signaling

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