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Compact archaeal variant of heme A synthase
Author(s) -
Lewin Anna,
Hederstedt Lars
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.080
Subject(s) - heme a , atp synthase , heme , bacillus subtilis , biochemistry , gene , biology , tandem exon duplication , gene duplication , enzyme , genetics , chemistry , bacteria
The N‐ and C‐terminal halves of the heme A synthase polypeptide of Bacillus subtilis , and many other organisms, are homologous. This indicates that these enzyme proteins originate from a tandem duplication and fusion event of a gene encoding a protein half as large. The ape1694 gene of the hyperthermophilic archaeon Aeropyrum pernix encodes a protein that is similar to the hypothetical small primordial protein. We demonstrate that this A. pernix protein is a heat‐stable membrane bound heme A synthase designated cCtaA. The case of cCtaA is unusual in evolution in that the primordial‐like protein has not become extinct and apparently carries out the same function as the twice as large more diversified heme A synthase protein variant found in most cytochrome a ‐containing organisms.