Abstract
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.
Original language | English |
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Pages (from-to) | 5351-5356 |
Journal | FEBS Letters |
Volume | 580 |
Issue number | 22 |
DOIs | |
Publication status | Published - 2006 |
Subject classification (UKÄ)
- Biological Sciences
Free keywords
- Aeropyrum
- protein evolution
- ape1694
- heme A synthesis
- CtaA
- cCtaA
- pernix