Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation

Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However t...

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Published inNature communications Vol. 11; no. 1; pp. 2846 - 11
Main Authors Branigan, Emma, Carlos Penedo, J., Hay, Ronald T.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.06.2020
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Abstract Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates. The mechanism of ubiquitin transfer from the ubiquitin-conjugated E2 enzyme (E2~Ub) to the substrate is still under debate. Here, the authors use FRET assays to show that RING E3 ligases transfer ubiquitin to the substrate from a closed E2~Ub conformation.
AbstractList Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates.
The mechanism of ubiquitin transfer from the ubiquitin-conjugated E2 enzyme (E2~Ub) to the substrate is still under debate. Here, the authors use FRET assays to show that RING E3 ligases transfer ubiquitin to the substrate from a closed E2~Ub conformation.
Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates. The mechanism of ubiquitin transfer from the ubiquitin-conjugated E2 enzyme (E2~Ub) to the substrate is still under debate. Here, the authors use FRET assays to show that RING E3 ligases transfer ubiquitin to the substrate from a closed E2~Ub conformation.
Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates.The mechanism of ubiquitin transfer from the ubiquitin-conjugated E2 enzyme (E2~Ub) to the substrate is still under debate. Here, the authors use FRET assays to show that RING E3 ligases transfer ubiquitin to the substrate from a closed E2~Ub conformation.
Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates.Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed conformation, where ubiquitin is folded back onto the E2 exposing the restrained thioester bond to attack by substrate nucleophile. However the proposal that the RING dependent closed conformation of E2~Ub represents the active form that mediates ubiquitin transfer has yet to be experimentally tested. To test this hypothesis we use single molecule Förster Resonance Energy Transfer (smFRET) to measure the conformation of a FRET labelled E2~Ub conjugate, which distinguishes between closed and alternative conformations. We describe a real-time FRET assay with a thioester linked E2~Ub conjugate to monitor single ubiquitination events and demonstrate that ubiquitin is transferred to substrate from the closed conformation. These findings are likely to be relevant to all RING E3 catalysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates.
ArticleNumber 2846
Author Carlos Penedo, J.
Branigan, Emma
Hay, Ronald T.
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  surname: Carlos Penedo
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Snippet Based on extensive structural analysis it was proposed that RING E3 ligases prime the E2~ubiquitin conjugate (E2~Ub) for catalysis by locking it into a closed...
The mechanism of ubiquitin transfer from the ubiquitin-conjugated E2 enzyme (E2~Ub) to the substrate is still under debate. Here, the authors use FRET assays...
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StartPage 2846
SubjectTerms 631/337/458/582
631/45/173
631/57/2265
Catalysis
Conformation
Conjugates
Crystallography, X-Ray
Efficiency
Energy transfer
Enzymes
Fluorescence Resonance Energy Transfer
Humanities and Social Sciences
Locking
multidisciplinary
Nuclear Proteins - metabolism
Protein Structure, Tertiary
Proteins
RING Finger Domains
Science
Science (multidisciplinary)
Single Molecule Imaging
Structural analysis
Substrates
Transcription Factors - metabolism
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
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  providerName: Springer Nature
Title Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation
URI https://link.springer.com/article/10.1038/s41467-020-16666-y
https://www.ncbi.nlm.nih.gov/pubmed/32503993
https://www.proquest.com/docview/2409865884
https://www.proquest.com/docview/2410368762
https://pubmed.ncbi.nlm.nih.gov/PMC7275055
https://doaj.org/article/804ead47bc3a4058bfc76e0bf7df8968
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