Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron–sulfur cluster binding
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.
Authors
- Yisong Guo (ORCID: https://orcid.org/0000-0002-4132-3565)
- Jin Xiong (ORCID: https://orcid.org/0000-0001-7443-0554)
- Jared Green
- Monika Tokmina‐Lukaszewska (ORCID: https://orcid.org/0000-0003-3298-8298)
- Brian Bothner (ORCID: https://orcid.org/0000-0003-1295-9609)
- James Larson (ORCID: https://orcid.org/0000-0001-9920-7682)
- Emily M. Dieter (ORCID: https://orcid.org/0009-0004-2294-9775)
- Joan Broderick (ORCID: https://orcid.org/0000-0001-7057-9124)
- William E. Broderick (ORCID: https://orcid.org/0000-0001-5782-7322)
Institutions
- Gettysburg College (US)
- Montana State University (US)
- Carnegie Mellon University (US)
Publication Details
- Journal
- FEBS Letters
- Published
- 2025-07-26
- DOI
- https://doi.org/10.1002/1873-3468.70120
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- U.S. Department of Energy
- M.J. Murdock Charitable Trust
- National Institutes of Health
- National Institute of General Medical Sciences
- Basic Energy Sciences