NDLI: NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80

Content Provider	Springer Nature Link
Author	Sekiyama, Naotaka Jee, JunGoo Isogai, Shin Akagi, Ken ichi Huang, Tai huang Ariyoshi, Mariko Tochio, Hidehito Shirakawa, Masahiro
Copyright Year	2012
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 recognition mechanism between the Lys63-linked diubiquitin (K63-Ub$_{2}$) and the tUIMs in solution, we determined the solution structure of the K63-Ub$_{2}$:tUIMs complex by using NOE restraints and RDC data derived from NMR spectroscopy. The structure showed that the tUIMs adopts a nearly straight and single continuous α-helix, and the two ubiquitin units of the K63-Ub$_{2}$ separately bind to each UIM motif. The interfaces are formed between Ile44-centered patches of the two ubiquitin units and the hydrophobic residues of the tUIMs. We also showed that the linker region between the two UIM motifs possesses a random-coil conformation in the free state, but undergoes the coil-to-helix transition upon complex formation, which simultaneously fixes the relative position of ubiquitin subunits. These data suggest that the relative position of ubiquitin subunits in the K63-Ub$_{2}$:tUIMs complex is essential for linkage-specific binding of Rap80 tUIMs.
Starting Page	339
Ending Page	350
Page Count	12
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	52
Issue Number	4
e-ISSN	15735001
Language	English
Publisher	Springer Netherlands
Publisher Date	2012-02-18
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ubiquitin Lys63-linked polyubiquitin chains Rap80 Tandem ubiquitin-interacting motifs NMR spectroscopy Biophysics and Biological Physics Biochemistry Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

NMR structure note: UBA domain of CIP75

NMR Assignment of Human Ubiquitin Conjugating Enzyme Ubc7

Structural analysis of the exopolysaccharide produced by Streptococcus thermophilus ST1 solely by NMR spectroscopy

Comprehensive Ubiquitin E2 Profiling of Ten Ubiquitin E3 Ligases

Conformational studies of antisense DNA by PFG NMR

In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes

Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy

NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80

Similar Documents

Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

NMR structure note: UBA domain of CIP75

NMR Assignment of Human Ubiquitin Conjugating Enzyme Ubc7

Structural analysis of the exopolysaccharide produced by Streptococcus thermophilus ST1 solely by NMR spectroscopy

Comprehensive Ubiquitin E2 Profiling of Ten Ubiquitin E3 Ligases

Conformational studies of antisense DNA by PFG NMR

In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes

Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy

NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80