A minimal SufB₂C₂ complex functions as a [4Fe-4S] cluster scaffold in methanogenic archaea.

ABSTRACT: Iron-sulfur clusters are essential cofactors in all domains of life, yet their biogenesis in obligately anaerobic archaea remains poorly understood. Here, we characterized the minimal two-protein SUF system in methanogenic archaea, composed solely of SufB and SufC. Using Methanococcus maripaludis as a model, we demonstrate that the SUF proteins from its native host form a stable SufB₂C₂ heterotetramer that binds a [4Fe-4S] cluster via three conserved cysteines in SufC. Mutations of conserved cysteine and histidine residues of SufB do not impair cluster binding. The complex interacts with the SAM-containing methanogenesis marker protein 10 (MmpX), suggesting direct Fe-S cluster transfer from SufB₂C₂ to target proteins. Mutational analysis o

SUBMITTER: Zhao C 

PROVIDER: S-EPMC12584684 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature