Compact archaeal variant of heme A synthase
(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:
https://lup.lub.lu.se/record/388470
- author
- Lewin, Anna LU and Hederstedt, Lars LU
- organization
- publishing date
- 2006
- 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
- 2022-01-28 08:33:23
@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}},
}