The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria. Issue 3 (25th December 2013)

• Record Type: Journal Article
• Authors: McNeil, Matthew B.; Hampton, Hannah G.; Hards, Kiel J.; Watson, Bridget N.J.; Cook, Gregory M.; Fineran, Peter C.
• Is Part Of: FEBS letters. Volume 588:Issue 3(2014)
• Page Start: 414
• Page End: 421
• Publication Date: 2013-12-25
• Subjects: FRD -- fumarate reductase -- SDH -- succinate dehydrogenase -- FAD -- flavin adenine dinucleotide -- Fumarate reductase -- FAD -- SDH5 -- SdhE -- Succinate dehydrogenase -- YgfY; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.12.019
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : The activity of the respiratory enzyme fumarate reductase (FRD) is dependent on the covalent attachment of the redox cofactor flavin adenine dinucleotide (FAD). We demonstrate that the FAD assembly factor SdhE, which flavinylates and activates the respiratory enzyme succinate dehydrogenase (SDH), is also required for the complete activation and flavinylation of FRD. SdhE interacted with, and flavinylated, the flavoprotein subunit FrdA, whilst mutations in a conserved RGxxE motif impaired the complete flavinylation and activation of FRD. These results are of widespread relevance because SDH and FRD play an important role in cellular energetics and are required for virulence in many important bacterial pathogens. Abstract : SdhE is required for the complete flavinylation and activation of FRD. SdhE interacts with and flavinylates the flavoprotein subunit FrdA. The RGxxE motif of SdhE is required for FRD activation.