Related ArticlesStructural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Chembiochem. 2019 Mar 28;:
Authors: Zhao X, Mißun M, Schneider T, Müller F, Lutz J, Scheffner M, Marx A, Kovermann M
Abstract
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. We recently established a facile, click chemistry-based approach for the efficient generation of linkage-defined Ub chains including Ub dimers. Within these chains, individual Ub moieties are connected via a triazole linkage rather than the natural isopeptide bond. Here, we report 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 high-resolution NMR spectroscopy. Thus, we conclude that artificially linked Ub dimers, as generated by our approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains.
PMID: 30920720 [PubMed - as supplied by publisher]
[NMR paper] The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif Related Articles The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
Biochem J. 2015 Oct 15;471(2):155-65
Authors: Wen Y, Shi L, Ding Y, Cui R, He WT, Hu HY,...
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[NMR paper] High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
Related Articles High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
Subcell Biochem. 2015;72:199-214
Authors: Kitahara R
Abstract
High-pressure nuclear magnetic resonance (NMR) spectroscopy has revealed that ubiquitin has at least two high-energy states - an alternatively folded state N2 and a locally disordered state I - between the basic folded state N1 and totally unfolded U...
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NMR Structure of the HumanRad18 Zinc Finger in Complexwith Ubiquitin Defines a Class of UBZ Domains in Proteins Linked tothe DNA Damage Response
NMR Structure of the HumanRad18 Zinc Finger in Complexwith Ubiquitin Defines a Class of UBZ Domains in Proteins Linked tothe DNA Damage Response
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500823h/20140915/images/medium/bi-2014-00823h_0006.gif
Biochemistry
DOI: 10.1021/bi500823h
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09-15-2014 07:13 PM
[NMR paper] NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
Biochemistry. 2014 Aug 27;
Authors: Rizzo AA, Salerno PE, Bezsonova I, Korzhnev DM
Abstract
Ubiquitin-mediated interactions are critical for the cellular DNA damage response (DDR). Therefore, many DDR-related proteins contain...
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08-28-2014 10:09 AM
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
Abstract Ubiquitin is a post-translational modifier that is involved in cellular functions through its covalent attachment to target proteins. Ubiquitin can also be conjugated to itself at seven lysine residues and at its amino terminus to form eight linkage-specific polyubiquitin chains for individual cellular processes. The Lys63-linked polyubiquitin chain is recognized by tandem ubiquitin-interacting motifs (tUIMs) of Rap80 for the regulation of DNA repair. To understand the...
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02-25-2012 12:16 AM
[NMR paper] Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Related Articles Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Proteins. 2005 Aug 15;60(3):367-81
Authors: van Dijk AD, Fushman D, Bonvin AM
When classical, Nuclear Overhauser Effect (NOE)-based approaches fail, it is possible, given high-resolution...
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12-01-2010 06:56 PM
[NMR paper] NMR structural studies of human cystatin C dimers and monomers.
NMR structural studies of human cystatin C dimers and monomers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structural studies of human cystatin C dimers and monomers.
J Mol Biol. 1997 Aug 15;271(2):266-77
Authors: Ekiel I, Abrahamson M, Fulton DB, Lindahl P, Storer AC, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, LeSauteur L, Gehring K
Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity...
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[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr
Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
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Biochemistry. 1995 Sep 12;34(36):11353-62
Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD
Arginine side chains are often...
Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Linear Mode
