By the same authors

From the same journal

From the same journal

Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development

Research output: Contribution to journalArticle

Standard

Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. / Rylott, E L; Rogers, C A; Gilday, A D; Edgell, T; Larson, T R; Graham, I A.

In: Journal of Biological Chemistry, Vol. 278, No. 24, 13.06.2003, p. 21370-21377.

Research output: Contribution to journalArticle

Harvard

Rylott, EL, Rogers, CA, Gilday, AD, Edgell, T, Larson, TR & Graham, IA 2003, 'Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development', Journal of Biological Chemistry, vol. 278, no. 24, pp. 21370-21377. https://doi.org/10.1074/jbc.M300826200

APA

Rylott, E. L., Rogers, C. A., Gilday, A. D., Edgell, T., Larson, T. R., & Graham, I. A. (2003). Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. Journal of Biological Chemistry, 278(24), 21370-21377. https://doi.org/10.1074/jbc.M300826200

Vancouver

Rylott EL, Rogers CA, Gilday AD, Edgell T, Larson TR, Graham IA. Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. Journal of Biological Chemistry. 2003 Jun 13;278(24):21370-21377. https://doi.org/10.1074/jbc.M300826200

Author

Rylott, E L ; Rogers, C A ; Gilday, A D ; Edgell, T ; Larson, T R ; Graham, I A. / Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 24. pp. 21370-21377.

Bibtex - Download

@article{10f8e0b5d5ed41e1b68aa00d9aa5d522,
title = "Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development",
abstract = "The short- chain acyl- CoA oxidase ( ACX4) is one of a family of ACX genes that together catalyze the first step of peroxisomal fatty acid beta- oxidation during early, post-germinative growth in oilseed species. Here we have isolated and characterized an Arabidopsis thaliana mutant containing a T- DNA insert in ACX4. In acx4 seedlings, short- chain acyl- CoA oxidase activity was reduced by greater than 98{\%}, whereas medium- chain activity was unchanged from wild type levels. Despite the almost complete loss of short- chain activity, lipid catabolism and seedling growth and establishment were unaltered in the acx4 mutant. However, the acx4 seedlings accumulated high levels ( 31 mol {\%}) of short- chain acyl- CoAs and showed resistance to 2,4- dichlorophenoxybutyric acid, which is converted to the herbicide and auxin analogue 2,4- dichlorophenoxyacetic acid by beta- oxidation. A mutant in medium- chain length acyl- CoA activity ( acx3) ( 1) shows a similar phenotype to acx4, and we show here that acx3 seedlings accumulate medium- chain length acyl- CoAs ( 16.4 mol {\%}). The acx3 and acx4 mutants were crossed together, and remarkably, the acx3acx4 double mutants aborted during the first phase of embryo development. We propose that acx3acx4 double mutants are nonviable because they have a complete block in short-chain acyl- CoA oxidase activity. This is the first demonstration of the effects of eliminating ( short- chain) beta- oxidation capacity in plants and shows that a functional beta- oxidation cycle is essential in the early stages of embryo development.",
keywords = "SACCHAROMYCES-CEREVISIAE, PEROXISOMAL PROTEINS, LIPID MOBILIZATION, SEED-GERMINATION, PLANTS, PATHWAYS, GENES, TRIACYLGLYCEROL, BIOSYNTHESIS, EXPRESSION",
author = "Rylott, {E L} and Rogers, {C A} and Gilday, {A D} and T Edgell and Larson, {T R} and Graham, {I A}",
year = "2003",
month = "6",
day = "13",
doi = "10.1074/jbc.M300826200",
language = "English",
volume = "278",
pages = "21370--21377",
journal = "The Journal of biological chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "24",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development

AU - Rylott, E L

AU - Rogers, C A

AU - Gilday, A D

AU - Edgell, T

AU - Larson, T R

AU - Graham, I A

PY - 2003/6/13

Y1 - 2003/6/13

N2 - The short- chain acyl- CoA oxidase ( ACX4) is one of a family of ACX genes that together catalyze the first step of peroxisomal fatty acid beta- oxidation during early, post-germinative growth in oilseed species. Here we have isolated and characterized an Arabidopsis thaliana mutant containing a T- DNA insert in ACX4. In acx4 seedlings, short- chain acyl- CoA oxidase activity was reduced by greater than 98%, whereas medium- chain activity was unchanged from wild type levels. Despite the almost complete loss of short- chain activity, lipid catabolism and seedling growth and establishment were unaltered in the acx4 mutant. However, the acx4 seedlings accumulated high levels ( 31 mol %) of short- chain acyl- CoAs and showed resistance to 2,4- dichlorophenoxybutyric acid, which is converted to the herbicide and auxin analogue 2,4- dichlorophenoxyacetic acid by beta- oxidation. A mutant in medium- chain length acyl- CoA activity ( acx3) ( 1) shows a similar phenotype to acx4, and we show here that acx3 seedlings accumulate medium- chain length acyl- CoAs ( 16.4 mol %). The acx3 and acx4 mutants were crossed together, and remarkably, the acx3acx4 double mutants aborted during the first phase of embryo development. We propose that acx3acx4 double mutants are nonviable because they have a complete block in short-chain acyl- CoA oxidase activity. This is the first demonstration of the effects of eliminating ( short- chain) beta- oxidation capacity in plants and shows that a functional beta- oxidation cycle is essential in the early stages of embryo development.

AB - The short- chain acyl- CoA oxidase ( ACX4) is one of a family of ACX genes that together catalyze the first step of peroxisomal fatty acid beta- oxidation during early, post-germinative growth in oilseed species. Here we have isolated and characterized an Arabidopsis thaliana mutant containing a T- DNA insert in ACX4. In acx4 seedlings, short- chain acyl- CoA oxidase activity was reduced by greater than 98%, whereas medium- chain activity was unchanged from wild type levels. Despite the almost complete loss of short- chain activity, lipid catabolism and seedling growth and establishment were unaltered in the acx4 mutant. However, the acx4 seedlings accumulated high levels ( 31 mol %) of short- chain acyl- CoAs and showed resistance to 2,4- dichlorophenoxybutyric acid, which is converted to the herbicide and auxin analogue 2,4- dichlorophenoxyacetic acid by beta- oxidation. A mutant in medium- chain length acyl- CoA activity ( acx3) ( 1) shows a similar phenotype to acx4, and we show here that acx3 seedlings accumulate medium- chain length acyl- CoAs ( 16.4 mol %). The acx3 and acx4 mutants were crossed together, and remarkably, the acx3acx4 double mutants aborted during the first phase of embryo development. We propose that acx3acx4 double mutants are nonviable because they have a complete block in short-chain acyl- CoA oxidase activity. This is the first demonstration of the effects of eliminating ( short- chain) beta- oxidation capacity in plants and shows that a functional beta- oxidation cycle is essential in the early stages of embryo development.

KW - SACCHAROMYCES-CEREVISIAE

KW - PEROXISOMAL PROTEINS

KW - LIPID MOBILIZATION

KW - SEED-GERMINATION

KW - PLANTS

KW - PATHWAYS

KW - GENES

KW - TRIACYLGLYCEROL

KW - BIOSYNTHESIS

KW - EXPRESSION

U2 - 10.1074/jbc.M300826200

DO - 10.1074/jbc.M300826200

M3 - Article

VL - 278

SP - 21370

EP - 21377

JO - The Journal of biological chemistry

JF - The Journal of biological chemistry

SN - 0021-9258

IS - 24

ER -