Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

• Main Authors: Cherak Stephana J., Turner Raymond J.
• Format: Article
• Language: English
• Published: De Gruyter 2017-09-01
• Series: Biomolecular Concepts
• Subjects: complex iron sulfur molybdoenzymes; dimethyl sulfoxide reductase; dmsd; maturation pathway; protein folding; system specific chaperone; twin-arginine translocase
• Online Access: https://doi.org/10.1515/bmc-2017-0011
• ISSN: 1868-5021; 1868-503X

Protein folding and assembly into macromolecule complexes within the living cell are complex processes requiring intimate coordination. The biogenesis of complex iron sulfur molybdoenzymes (CISM) requires use of a system specific chaperone – a redox enzyme maturation protein (REMP) – to help mediate final folding and assembly. The CISM dimethyl sulfoxide (DMSO) reductase is a bacterial oxidoreductase that utilizes DMSO as a final electron acceptor for anaerobic respiration. The REMP DmsD strongly interacts with DMSO reductase to facilitate folding, cofactor-insertion, subunit assembly and targeting of the multi-subunit enzyme prior to membrane translocation and final assembly and maturation into a bioenergetic catalytic unit. In this article, we discuss the biogenesis of DMSO reductase as an example of the participant network for bacterial CISM maturation pathways.