Evidence map›Paper›PMID 27411375›Full record

ArticleScientific reports2016

A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125.

Marie-José Bijlmakers, João M C Teixeira, Roeland Boer, Maxim Mayzel, Pilar Puig-Sàrries, Göran Karlsson, Miquel Coll, Miquel Pons, Bernat Crosas

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Marie-José BijlmakersInstitut de Biologia Molecular de Barcelona, CSIC, Parc Cientific de Barcelona, 08028 Barcelona, Spain.
João M C TeixeiraBioNMR Laboratory, Inorganic and Organic Chemistry Department, Organic Chemistry Section, University of Barcelona, Parc Cientific de Barcelona, 08028 Barcelona, Spain.
Roeland BoerXALOC beamline, ALBA synchrotron (CELLS), 08290 Cerdanyola del Valles, Spain.
Maxim MayzelSwedish NMR Centre, University of Gothenburg, SE-40530, Gothenburg, Sweden.
Pilar Puig-SàrriesInstitut de Biologia Molecular de Barcelona, CSIC, Parc Cientific de Barcelona, 08028 Barcelona, Spain.
Göran KarlssonSwedish NMR Centre, University of Gothenburg, SE-40530, Gothenburg, Sweden.
Miquel CollInstitut de Biologia Molecular de Barcelona, CSIC, Parc Cientific de Barcelona, 08028 Barcelona, Spain.
Miquel PonsBioNMR Laboratory, Inorganic and Organic Chemistry Department, Organic Chemistry Section, University of Barcelona, Parc Cientific de Barcelona, 08028 Barcelona, Spain.
Bernat CrosasInstitut de Biologia Molecular de Barcelona, CSIC, Parc Cientific de Barcelona, 08028 Barcelona, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING domain and ubiquitin conjugating enzymes (E2), but posttranslational events or additional structural elements, yet largely undefined, are frequently required to enhance or regulate activity. Here, we show for the ubiquitin ligase RNF125 that, in addition to the RING domain, a C2HC Zn finger (ZnF) is crucial for activity, and a short linker sequence (Li2(120-128)) enhances activity. The contribution of these regions was first shown with truncated proteins, and the essential role of the ZnF was confirmed with mutations at the Zn chelating Cys residues. Using NMR, we established that the C2HC ZnF/Li2(120-128) region is crucial for binding of the RING domain to the E2 UbcH5a. The partial X-ray structure of RNF125 revealed the presence of extensive intramolecular interactions between the RING and C2HC ZnF. A mutation at one of the contact residues in the C2HC ZnF, a highly conserved M112, resulted in the loss of ubiquitin ligase activity. Thus, we identified the structural basis for an essential role of the C2HC ZnF and conclude that this domain stabilizes the RING domain, and is therefore required for binding of RNF125 to an E2.

Indexed as

Amino Acid SequenceCrystallography, X-RayHEK293 CellsHumansModels, MolecularMutant ProteinsPoint MutationProtein BindingProtein DomainsStructure-Activity RelationshipUbiquitinUbiquitin-Protein LigasesZinc FingersMutant ProteinsRNF125 protein, humanUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID27411375
PMCPMC4944129

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.