Evidence map›Paper›PMID 40715996›Full record

ArticleFEBS letters2025

Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron-sulfur cluster binding.

Emily M Dieter, James Larson, Monika Tokmina-Lukaszewska, Jin Xiong, Jared Green, Yisong Guo, William E Broderick, Brian Bothner, Joan B Broderick

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Emily M DieterDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
James LarsonDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
Monika Tokmina-LukaszewskaDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
Jin XiongDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, USA.
Jared GreenDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
Yisong GuoDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, USA.
William E BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
Brian BothnerDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.
Joan B BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA.ORCID https://orcid.org/0000-0001-7057-9124

Funding

Research Core (Developmental Research Project Program)P20GM103474 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI Ann Therese Bertagnolli · 2012 to 2026
$60.0M
Elucidate Mechanisms of Quinolone Alkaloid Biosynthesis via Iron(II)/2-Oxoglutarate Dependent Enzymes: Diverse, but Controlled ReactivityR01GM125924 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI Yisong Guo · 2018 to 2026
$3.3M
Ultra Performance Liquid Chromatography Tandem Mass Spectrometer for MetabolomicsS10OD028650 · OD · MONTANA STATE UNIVERSITY - BOZEMAN · PI BOTHNER, BRIAN P · 2020 to 2020
$599k
Basic Energy Sciences DE-SC0020246NIGMS NIH HHS P20 GM103474NIGMS NIH HHS R01 GM125924NIGMS NIH HHS R01GM125924NIH HHS S10 OD028650
6 · The paper itself

Abstract

Methanogenic archaea are particularly rich in iron-sulfur proteins, yet their roles remain largely enigmatic. Here, we characterized a Methanococcus voltae (Mvo) protein from the domain of unknown function (DUF) 2193 family, a group of proteins present primarily in archaea and characterized by a conserved cysteine-rich C-terminal motif. MvoDUF2193 was heterologously expressed and characterized by a range of spectroscopic and analytical methods. The results demonstrate that MvoDUF2193 binds a single [4Fe-4S] cluster per subunit and that cluster occupancy regulates the transition from an apo tetramer to a [4Fe-4S] monomeric form. We hypothesize that MvoDUF2193 serves a regulatory role in the cell, mediated by [Fe-S] cluster binding and changes in oligomeric state.

Indexed as

Archaeal ProteinsIron-Sulfur ProteinsMethanococcusAmino Acid SequenceProtein BindingProtein DomainsProtein MultimerizationArchaeal ProteinsIron-Sulfur Proteinsallosterycellular redox statusDUF2193Fe/S clustersion mobility native mass spectrometrymethanogens

Identifiers

PMID40715996
PMCPMC12375889

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Registered trials

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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.