Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase ofEscherichia coli

Darlison, M G; Guest, J R

Abstract

The nucleotide sequence of a 961 base-pair segment of DNA containing the sdhB gene, which encodes the iron-sulphur protein subunit of the E. coli succinate dehydrogenase, has been determined. The sdhB structural gene comprises 711 base pairs (237 codons, excluding the translational initiator and terminator). It is separated by a 15 base-pair intergenic region from the preceding flavoprotein gene (sdhA) and is the distal gene of an operon that also includes genes (sdhC and D) encoding two hydrophobic subunits, sdhCDAB. The distal end of the sdh operon is linked to the 2-oxoglutarate dehydrogenase gene (sucA) by a complex region of dyad symmetry that is homologous with several potential intercistronic regulatory elements or transcriptional attenuators. The sdhB structural gene encodes a polypeptide of Mr26637 that is strikingly homologous with the iron-sulphur protein subunit of fumarate reductase (38% identity, increasing to 58% when conservative changes are included). Both subunits contain 11 cysteine residues, 10 being conserved in three clusters resembling those found in ferredoxins. This work completes the sequence of a 9897 base-pair segment of DNA containing seven tricarboxylic acid cycle genes encoding three enzymes or enzyme complexes, citrate synthase (gltA), succinate dehydrogenase (sdh), and the 2-oxoglutarate dehydrogenase complex (suc), that are organized thus: gltA-sdhCDAB-sucAB.

Citation

Darlison, M. G., & Guest, J. R. (1984). Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase ofEscherichia coli. Biochemical Journal, 223(2), 507-517. https://doi.org/10.1042/bj2230507

• Journal Article Type: Article
• Online Publication Date: Oct 15, 1984
• Publication Date: Oct 15, 1984
• Deposit Date: Jul 26, 2016
• Journal: Biochemical Journal
• Print ISSN: 0264-6021
• Electronic ISSN: 1470-8728
• Publisher: Portland Press
• Peer Reviewed: Peer Reviewed
• Volume: 223
• Issue: 2
• Pages: 507-517
• DOI: https://doi.org/10.1042/bj2230507
• Keywords: Cell Biology; Biochemistry; Molecular Biology
• Public URL: http://researchrepository.napier.ac.uk/Output/317013