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Compact archaeal variant of heme A synthase

På svenska

Author

Summary, in English

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.

Publishing year

2006

Language

English

Pages

5351-5356

Publication/Series

FEBS Letters

Volume

580

Issue

22

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences

Keywords

  • Aeropyrum
  • protein evolution
  • ape1694
  • heme A synthesis
  • CtaA
  • cCtaA
  • pernix

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-3468