Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Compact archaeal variant of heme A synthase

Lewin, Anna LU and Hederstedt, Lars LU (2006) In FEBS Letters 580(22). p.5351-5356
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Aeropyrum, protein evolution, ape1694, heme A synthesis, CtaA, cCtaA, pernix
in
FEBS Letters
volume
580
issue
22
pages
5351 - 5356
publisher
Wiley-Blackwell
external identifiers
  • pmid:16989823
  • wos:000241044400038
  • scopus:33748783370
ISSN
1873-3468
DOI
10.1016/j.febslet.2006.08.080
language
English
LU publication?
yes
id
643ffe91-476b-4dae-93b7-0fa4fda8090f (old id 388470)
date added to LUP
2016-04-01 15:59:34
date last changed
2025-10-14 13:08:28
@article{643ffe91-476b-4dae-93b7-0fa4fda8090f,
  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.}},
  author       = {{Lewin, Anna and Hederstedt, Lars}},
  issn         = {{1873-3468}},
  keywords     = {{Aeropyrum; protein evolution; ape1694; heme A synthesis; CtaA; cCtaA; pernix}},
  language     = {{eng}},
  number       = {{22}},
  pages        = {{5351--5356}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Compact archaeal variant of heme A synthase}},
  url          = {{http://dx.doi.org/10.1016/j.febslet.2006.08.080}},
  doi          = {{10.1016/j.febslet.2006.08.080}},
  volume       = {{580}},
  year         = {{2006}},
}