STRUCTURAL ORGANIZATION OF THE GENE ENCODING THE HUMAN IRON-SULFUR SUBUNIT OF SUCCINATE-DEHYDROGENASE

The iron-sulfur protein (Ip) subunit of succinate dehydrogenase (SDH a nd complex II) of the respiratory chain is highly conserved in evoluti on [Gould et al., Proc. Natl. Acad, Sci. USA 86 (1989) 1934-1938]. We have cloned the entire human Ip cDNA, as well as the Ip-encoding gene (SDH-B) from two genomic human libraries. The cDNA contains a coding s equence of 840 nt, flanked by a 5'-UTR of 133 nt and a 3'-UTR of 123 n t. The entire transcript is encoded by eight exons within approx. 40 k b, The seven introns range in size from 0.75 kb to >11 kb, and they ap pear to be of the 'late' intron class, Approx. 5 kb of upstream sequen ce was also cloned, and approx. 2.4 kb of the promoter region were seq uenced and analyzed for consensus elements binding potential transcrip tion factors and transcriptional activators.