Biopolym. Cell. 1988; 4(5):238-245.
http://dx.doi.org/10.7124/bc.000231
Structure and Function of Biopolymers
Possibility of iron-sulfur proteins coding in mammalian mitochondrial genome
1Beregovskaya N. N., 1Savich A. V.
  1. Institute of Biophysics, Ministry of Public Health of the USSR
    Moscow, USSR

Abstract

Comparison of amino acid sequences of proteins coded on unidentified replication frames (URF) of human mitochondrial genome with those of bacterial iron-sulfur and flavo-proteins showed their resemblance. On this basis an evolutionary scheme of relationships between proteins of this kind is presented.
Full text: (PDF, in Russian)

References

[1] Nomenclature of iron-sulfur proteins. Recommendations, 1978: Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Biochim Biophys Acta. 1979;549(2):101-5.
[2] George DG, Hunt LT, Yeh LS, Barker WC. New perspectives on bacterial ferredoxin evolution. J Mol Evol. 1985;22(1):20-31.
[3] Beinert H. Iron-sulfur proteins, the most numerous and most diversified components of the mitochondrial electron transfer system. Adv Exp Med Biol. 1976;74:137-49.
[4] Chance B. Electron transfer: pathways, mechanisms, and controls. Annu Rev Biochem. 1977;46:967-80.
[5] Luzikov VI. Regulation of the mitochondria formation. Moscow, Nauka, 1980; 318 p.
[6] Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG. Sequence and organization of the human mitochondrial genome. Nature. 1981;290(5806):457-65.
[7] DePierre JW, Ernster L. Enzyme topology of intracellular membranes. Annu Rev Biochem. 1977;46:201-62.
[8] Cole ST, Grundstr?m T, Jaurin B, Robinson JJ, Weiner JH. Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem. 1982;126(1):211-6.
[9] Young IG, Rogers BL, Campbell HD, Jaworowski A, Shaw DC. Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon. Eur J Biochem. 1981;116(1):165-70.
[10] Cole ST. Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem. 1982;122(3):479-84.
[11] Commak R. Evolution and diversity in the iron-sulfur proteins. Chim Scr. 1983. 21(1):87-95.
[12] Dayhoff M. O., Hunt T. L. Protein sequence database. Washington: D. C., 1981. 265 p.
[13] Dayhoff MO, Barker WC, Hunt LT. Establishing homologies in protein sequences. Methods Enzymol. 1983;91:524-45.
[14] Tedro SM, Meyer TE, Kamen MD. Primary structure of a high potential iron-sulfur protein from the photosynthetic bacterium Thiocapsa pfennigii. J Biol Chem. 1974;249(4):1182-8.
[15] Fox J. L. Evolution of flavo proteins. Flavins and flavoproteins. Amsterdam: Elsevier, 1976. :432-436.
[16] Kagi JH, Kojima Y, Kissling MM, Lerch K. Metallothionein: an exceptional metal thiolate protein. Ciba Found Symp. 1979;(72):223-37.