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FEBS Lett. 2014 Jan 31;588(3):414-21. doi: 10.1016/j.febslet.2013.12.019. Epub 2013 Dec 25.

The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria.

Author information

1
Department of Microbiology and Immunology, University of Otago, PO Box 56, Dunedin 9054, New Zealand.
2
Department of Microbiology and Immunology, University of Otago, PO Box 56, Dunedin 9054, New Zealand. Electronic address: peter.fineran@otago.ac.nz.

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.

KEYWORDS:

FAD; FRD; Fumarate reductase; SDH; SDH5; SdhE; Succinate dehydrogenase; YgfY; flavin adenine dinucleotide; fumarate reductase; succinate dehydrogenase

PMID:
24374335
DOI:
10.1016/j.febslet.2013.12.019
[Indexed for MEDLINE]
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