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  Multifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases

Chrustowicz, J., Sherpa, D., Teyra, J., Loke, M. S., Popowicz, G. M., Basquin, J., et al. (2022). Multifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases. Journal of Molecular Biology, 434(2): 167347. doi:10.1016/j.jmb.2021.167347.

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1-s2.0-S0022283621005842-main.pdf (Publisher version), 4MB
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 Creators:
Chrustowicz, Jakub1, Author              
Sherpa, Dawafuti1, Author              
Teyra, Joan2, Author
Loke, Mun Siong1, Author
Popowicz, Grzegorz M.2, Author
Basquin, Jerome2, Author
Sattler, Michael2, Author
Prabu, J. Rajan1, Author              
Sidhu, Sachdev S.2, Author
Schulman, Brenda1, Author              
Affiliations:
1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              
2external, ou_persistent22              

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Free keywords: END RULE PATHWAY; UBIQUITIN-PROTEASOME SYSTEM; STRUCTURAL BASIS; CATABOLITE DEGRADATION; TERMINAL ACETYLATION; GID COMPLEX; SUBSTRATE RECOGNITION; PROTEIN-QUALITY; MOLECULAR-BASIS; PHAGE DISPLAYBiochemistry & Molecular Biology; N-degron pathway; Phage display; Ubiquitin; Protein-protein interaction; Structural biology;
 Abstract: N-degron E3 ubiquitin ligases recognize specific residues at the N-termini of substrates. Although molecular details of N-degron recognition are known for several E3 ligases, the range of N-terminal motifs that can bind a given E3 substrate binding domain remains unclear. Here, we discovered capacity of Gid4 and Gid10 substrate receptor subunits of yeast "GID"/human "CTLH" multiprotein E3 ligases to tightly bind a wide range of N-terminal residues whose recognition is determined in part by the downstream sequence context. Screening of phage displaying peptide libraries with exposed N-termini identified novel consensus motifs with non-Pro N-terminal residues binding Gid4 or Gid10 with high affinity. Structural data reveal that conformations of flexible loops in Gid4 and Gid10 complement sequences and folds of interacting peptides. Together with analysis of endogenous substrate degrons, the data show that degron identity, substrate domains harboring targeted lysines, and varying E3 ligase higher-order assemblies combinatorially determine efficiency of ubiquitylation and degradation. (c) 2021 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

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Language(s): eng - English
 Dates: 2022-01-30
 Publication Status: Published online
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000725064200007
DOI: 10.1016/j.jmb.2021.167347
 Degree: -

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Title: Journal of Molecular Biology
  Other : JMB
  Abbreviation : J. Mol. Biol.
Source Genre: Journal
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Publ. Info: Elsevier
Pages: - Volume / Issue: 434 (2) Sequence Number: 167347 Start / End Page: - Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/0022-2836