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  Reconstitution and structural analysis of a HECT ligase-ubiquitin complex via an activity-based probe

Nair, R. M., Seenivasan, A., Liu, B., Chen, D., Lowe, E. D., & Lorenz, S. (2021). Reconstitution and structural analysis of a HECT ligase-ubiquitin complex via an activity-based probe. ACS Chemical Biology, 16(9), 1615-1621. doi:10.1021/acschembio.1c00433.

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Nair, R. M., Author
Seenivasan, A.1, Author           
Liu, B., Author
Chen, D., Author
Lowe, E. D., Author
Lorenz, S.1, Author           
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1Research Group Ubiquitin Signaling Specificity, MPI for Biophysical Chemistry, Max Planck Society, ou_3337583              

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 Abstract: Ubiquitin activity-based probes have proven invaluable in elucidating structural mechanisms in the ubiquitin system by stabilizing transient macromolecular complexes of deubiquitinases, ubiquitin-activating enzymes, and the assemblies of ubiquitin-conjugating enzymes with ubiquitin ligases of the RING-Between-RING and RING-Cysteine-Relay families. Here, we demonstrate that an activity-based probe, ubiquitin-propargylamine, allows for the preparative reconstitution and structural analysis of the interactions between ubiquitin and certain HECT ligases. We present a crystal structure of the ubiquitin-linked HECT domain of HUWE1 that defines a catalytically critical conformation of the C-terminal tail of the ligase for the transfer of ubiquitin to an acceptor protein. Moreover, we observe that ubiquitin-propargylamine displays selectivity among HECT domains, thus corroborating the notion that activity-based probes may provide entry points for the development of specific, active site-directed inhibitors and reporters of HECT ligase activities.

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Language(s): eng - English
 Dates: 2021-08-17
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acschembio.1c00433
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Title: ACS Chemical Biology
Source Genre: Journal
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Pages: - Volume / Issue: 16 (9) Sequence Number: - Start / End Page: 1615 - 1621 Identifier: -