Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron–sulfur cluster binding
Year: 2025
Type: article
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.
Source: FEBS Letters
Language: English
Field: Energy
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,980
Awards: G1410756938, PROBING NOVEL PATHWAYS OF IRON SULFIDE ACQUISITION AND TRAFFICKING IN MODEL BIOCATALYTIC SYSTEMS, G2744771272, Ultra Performance Liquid Chromatography Tandem Mass Spectrometer for Metabolomics, G4539748024, G4933603664, G515965682, G8306589951, G9000081922, Dissect Mechanism of Iron(II)/2-Oxoglutarate Dependent Enzymes Catalyzed Halogenation in Nucleotide Biosynthesis
OpenAlex ID: W4412664137