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  Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation

Fulda, M., Shockey, J., Werber, M., Wolter, F. P., & Heinz, E. (2002). Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation. Plant Journal, 32(1), 93-103.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D7D-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D7E-E
Genre: Journal Article

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 Creators:
Fulda, M., Author
Shockey, J., Author
Werber, M.1, Author              
Wolter, F. P., Author
Heinz, E., Author
Affiliations:
1ADIS, MPI for Plant Breeding Research, Max Planck Society, ou_1113564              

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Free keywords: acyl-CoA synthetase; beta-oxidation; Arabidopsis; peroxisomal targeting
 Abstract: Post-germinative growth of oilseeds is dependent on the breakdown of the stored lipid reserves. Long-chain acyl-CoA synthetase activities (LACS) are critically involved in this process by activating the released free fatty acids and thus feeding the beta-oxidation cycle in glyoxysomes. Here we report on the identification of two LACS genes, AtLACS6 and AtLACS7 from Arabidopsis thaliana coding for peroxisomal LACS proteins. The subcellular localization was verified by co-expression studies of spectral variants of the green fluorescent protein (GFP). While AtLACS6 is targeted by a type 2 (PTS2) peroxisomal targeting sequence, for AtLACS7 a functional PTS1 as well as a PTS2 could be demonstrated. Possible explanations for this potentially redundant targeting information will be discussed. Expression studies of both genes revealed a strong induction 1 day after germination resembling the expression pattern of other genes involved in beta-oxidation. Analysis of the substrate specificities of the two LACS proteins demonstrated enzymatic activity for both enzymes with the whole spectrum of fatty acids found in stored lipid reserves. These results suggest that both LACS proteins might have overlapping functions and are able to initiate beta-oxidation in plant peroxisomes.

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Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 127756
ISI: 000178374100008
 Degree: -

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Title: Plant Journal
  Alternative Title : Plant J.
Source Genre: Journal
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Pages: - Volume / Issue: 32 (1) Sequence Number: - Start / End Page: 93 - 103 Identifier: ISSN: 0960-7412