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The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment

Elizabeth L. Rylott, Peter J. Eastmond, Alison D. Gilday, Steve Slocombe, Tony R. Larson, Alison Baker, Ian A. Graham

The Plant Journal, Volume: 45, Issue: 6, Pages: 930 - 941

Swansea University Author: Steve Slocombe

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DOI (Published version): 10.1111/j.1365-313x.2005.02650.x

Abstract

The multifunctional protein (MFP) of peroxisomal beta-oxidation catalyses four separate reactions, two of which (2-trans enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase) are core activities required for the catabolism of all fatty acids. We have isolated and characterized five Arabidopsis...

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Published in: The Plant Journal
ISSN: 0960-7412 1365-313X
Published: Wiley 2006
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URI: https://cronfa.swan.ac.uk/Record/cronfa65482
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spelling v2 65482 2024-01-22 The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment 4a1ea486a78ed357efdfa053a277ae40 Steve Slocombe Steve Slocombe true false 2024-01-22 SBI The multifunctional protein (MFP) of peroxisomal beta-oxidation catalyses four separate reactions, two of which (2-trans enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase) are core activities required for the catabolism of all fatty acids. We have isolated and characterized five Arabidopsis thaliana mutants in the MFP2 gene that is expressed predominantly in germinating seeds. Seedlings of mfp2 require an exogenous supply of sucrose for seedling establishment to occur. Analysis of mfp2-1 seedlings revealed that seed storage lipid was catabolized more slowly, long-chain acyl-CoA substrates accumulated and there was an increase in peroxisome size. Despite a reduction in the rate of beta-oxidation, mfp2 seedlings are not resistant to the herbicide 2,4-dichlorophenoxybutyric acid, which is catabolized to the auxin 2,4-dichlorophenoxyacetic acid by beta-oxidation. Acyl-CoA feeding experiments show that the MFP2 2-trans enoyl-CoA hydratase only exhibits activity against long chain (C18:0) substrates, whereas the MFP2 L-3-hydroxyacyl-CoA dehydrogenase is active on C6:0, C12:0 and C18:0 substrates. A mutation in the abnormal inflorescence meristem gene AIM1, the only homologue of MFP2, results in an abnormal inflorescence meristem phenotype in mature plants (Richmond and Bleecker, Plant Cell 11, 1999, 1911) demonstrating that the role of these genes is very different. The mfp2-1 aim1double mutant aborted during the early stages of embryo development showing that these two proteins share a common function that is essential for this key stage in the life cycle. Journal Article The Plant Journal 45 6 930 941 Wiley 0960-7412 1365-313X β-oxidation; Arabidopsis; multifunctional protein; hydratase; dehydrogenase 1 3 2006 2006-03-01 10.1111/j.1365-313x.2005.02650.x COLLEGE NANME Biosciences COLLEGE CODE SBI Swansea University 2024-03-21T17:03:00.0799421 2024-01-22T14:07:07.5704565 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Biosciences Elizabeth L. Rylott 1 Peter J. Eastmond 2 Alison D. Gilday 3 Steve Slocombe 4 Tony R. Larson 5 Alison Baker 6 Ian A. Graham 7
title The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
spellingShingle The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
Steve Slocombe
title_short The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
title_full The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
title_fullStr The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
title_full_unstemmed The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
title_sort The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
author_id_str_mv 4a1ea486a78ed357efdfa053a277ae40
author_id_fullname_str_mv 4a1ea486a78ed357efdfa053a277ae40_***_Steve Slocombe
author Steve Slocombe
author2 Elizabeth L. Rylott
Peter J. Eastmond
Alison D. Gilday
Steve Slocombe
Tony R. Larson
Alison Baker
Ian A. Graham
format Journal article
container_title The Plant Journal
container_volume 45
container_issue 6
container_start_page 930
publishDate 2006
institution Swansea University
issn 0960-7412
1365-313X
doi_str_mv 10.1111/j.1365-313x.2005.02650.x
publisher Wiley
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Biosciences, Geography and Physics - Biosciences{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Biosciences
document_store_str 0
active_str 0
description The multifunctional protein (MFP) of peroxisomal beta-oxidation catalyses four separate reactions, two of which (2-trans enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase) are core activities required for the catabolism of all fatty acids. We have isolated and characterized five Arabidopsis thaliana mutants in the MFP2 gene that is expressed predominantly in germinating seeds. Seedlings of mfp2 require an exogenous supply of sucrose for seedling establishment to occur. Analysis of mfp2-1 seedlings revealed that seed storage lipid was catabolized more slowly, long-chain acyl-CoA substrates accumulated and there was an increase in peroxisome size. Despite a reduction in the rate of beta-oxidation, mfp2 seedlings are not resistant to the herbicide 2,4-dichlorophenoxybutyric acid, which is catabolized to the auxin 2,4-dichlorophenoxyacetic acid by beta-oxidation. Acyl-CoA feeding experiments show that the MFP2 2-trans enoyl-CoA hydratase only exhibits activity against long chain (C18:0) substrates, whereas the MFP2 L-3-hydroxyacyl-CoA dehydrogenase is active on C6:0, C12:0 and C18:0 substrates. A mutation in the abnormal inflorescence meristem gene AIM1, the only homologue of MFP2, results in an abnormal inflorescence meristem phenotype in mature plants (Richmond and Bleecker, Plant Cell 11, 1999, 1911) demonstrating that the role of these genes is very different. The mfp2-1 aim1double mutant aborted during the early stages of embryo development showing that these two proteins share a common function that is essential for this key stage in the life cycle.
published_date 2006-03-01T17:03:00Z
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score 11.0133505

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