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Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli

Doan, Thuy T. P. ; Carlsson, Anders S. ; Hamberg, Mats ; Bülow, Leif LU ; Stymne, Sten and Olsson, Peter LU orcid (2009) In Journal of Plant Physiology 166(8). p.787-796
Abstract
Very long chain primary alcohols are significant components in cuticle waxes of plants. Fatty acyl-CoA reductases (FARs) catalyze the formation of a fatty alcohol from an acyl-CoA. The Arabidopsis (Arabidopsis thaliana) genome contains eight genes homologous to FAR genes from jojoba (Simmondsia chinensis), silk moth, wheat and mouse. Expression of six Arabidopsis FAR homologs in Escherichia coli resulted in production of alcohols from endogenous E. coli fatty acids by five of these genes, confirming that they encode for FAR enzymes. Only a truncated splicing version of the sixth gene was found, and this gene yielded a protein with no FAR activity. The five functional FAR enzymes yielded distinctly different compositions of fatty alcohols... (More)
Very long chain primary alcohols are significant components in cuticle waxes of plants. Fatty acyl-CoA reductases (FARs) catalyze the formation of a fatty alcohol from an acyl-CoA. The Arabidopsis (Arabidopsis thaliana) genome contains eight genes homologous to FAR genes from jojoba (Simmondsia chinensis), silk moth, wheat and mouse. Expression of six Arabidopsis FAR homologs in Escherichia coli resulted in production of alcohols from endogenous E. coli fatty acids by five of these genes, confirming that they encode for FAR enzymes. Only a truncated splicing version of the sixth gene was found, and this gene yielded a protein with no FAR activity. The five functional FAR enzymes yielded distinctly different compositions of fatty alcohols when expressed in E. coli, indicating that the different enzymes may be involved in the production of different types of alcohols in plant cells. (C) 2008 Elsevier GmbH. All rights reserved. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
NAD(P)H, Jojoba, Fatty acyl-CoA reductase, Fatty alcohol, Wax ester
in
Journal of Plant Physiology
volume
166
issue
8
pages
787 - 796
publisher
Gustav Fischer Verlag
external identifiers
  • wos:000266302700001
  • scopus:65049083862
  • pmid:19062129
ISSN
0176-1617
DOI
10.1016/j.jplph.2008.10.003
language
English
LU publication?
yes
id
3520945c-af39-4331-96c7-8738786b3015 (old id 1425621)
date added to LUP
2016-04-01 14:13:46
date last changed
2022-04-22 02:07:08
@article{3520945c-af39-4331-96c7-8738786b3015,
  abstract     = {{Very long chain primary alcohols are significant components in cuticle waxes of plants. Fatty acyl-CoA reductases (FARs) catalyze the formation of a fatty alcohol from an acyl-CoA. The Arabidopsis (Arabidopsis thaliana) genome contains eight genes homologous to FAR genes from jojoba (Simmondsia chinensis), silk moth, wheat and mouse. Expression of six Arabidopsis FAR homologs in Escherichia coli resulted in production of alcohols from endogenous E. coli fatty acids by five of these genes, confirming that they encode for FAR enzymes. Only a truncated splicing version of the sixth gene was found, and this gene yielded a protein with no FAR activity. The five functional FAR enzymes yielded distinctly different compositions of fatty alcohols when expressed in E. coli, indicating that the different enzymes may be involved in the production of different types of alcohols in plant cells. (C) 2008 Elsevier GmbH. All rights reserved.}},
  author       = {{Doan, Thuy T. P. and Carlsson, Anders S. and Hamberg, Mats and Bülow, Leif and Stymne, Sten and Olsson, Peter}},
  issn         = {{0176-1617}},
  keywords     = {{NAD(P)H; Jojoba; Fatty acyl-CoA reductase; Fatty alcohol; Wax ester}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{787--796}},
  publisher    = {{Gustav Fischer Verlag}},
  series       = {{Journal of Plant Physiology}},
  title        = {{Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli}},
  url          = {{http://dx.doi.org/10.1016/j.jplph.2008.10.003}},
  doi          = {{10.1016/j.jplph.2008.10.003}},
  volume       = {{166}},
  year         = {{2009}},
}