The Arabidopsis acn (acetate non-utilizing) mutants were isolated by fluoroacetate-resistant germination and seedling establishment. We report the characterization of the acn2 mutant. Physiological analyses of acn2 showed that it possessed characteristics similar to those of the mutants cts (COMATOSE)-1 and pxa [peroxisomal ABC (ATP-binding-cassette) transporter]1. The acn2 locus was mapped to within 3 cM of the CTS gene on the bottom arm of chromosome IV using CAPS (cleavage amplification polymorphism) and SSLP (simple sequence-length polymorphism) markers. Crossing acn2 and cts-1 failed to restore the fluoroacetate-sensitive phenotype, suggesting that these mutations were allelic. Sequencing of the ACN2 locus revealed a C→T nonsense mutation in exon 13, which would have resulted in the elimination of the C-terminal hemitransporter domain of the encoded protein. Neither the full-length CTS protein nor the truncated protein was detected on immunoblots using either C-terminal- or N-terminal-specific anti-CTS antibodies respectively, demonstrating the absence of the entire CTS protein in acn2 mutants. Emerged seedlings of both cts-1 and pxa1 alleles displayed increased resistance to FAc (monofluoroacetic acid) compared with the corresponding wild-type seedlings. Complementation studies showed that mutation of the CTS gene was responsible for the FAc-resistant phenotype, as when the wild-type protein was expressed in both the cts-1 and pxa1 mutant lines, the strains became FAc-sensitive. Feeding studies confirmed that both acn2 and cts-1 mutants were compromised in their ability to convert radiolabelled acetate into soluble carbohydrate. These results demonstrate a role for the ABC protein CTS in providing acetate to the glyoxylate cycle in developing seedlings.
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September 2007
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Research Article|
August 29 2007
The Arabidopsis ALDP protein homologue COMATOSE is instrumental in peroxisomal acetate metabolism
Mark A. Hooks;
Mark A. Hooks
1
*School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, U.K.
1To whom correspondence should be addressed (email m.a.hooks@bangor.ac.uk).
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James E. Turner;
James E. Turner
*School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, U.K.
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Elaine C. Murphy;
Elaine C. Murphy
*School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, U.K.
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Katherine A. Johnston;
Katherine A. Johnston
†Centre for Plant Sciences, Irene Manton Building, University of Leeds, Leeds LS2 9JT, U.K.
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Sally Burr;
Sally Burr
2
*School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, U.K.
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Szymon Jarosławski
Szymon Jarosławski
*School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, U.K.
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Publisher: Portland Press Ltd
Received:
February 19 2007
Revision Received:
June 20 2007
Accepted:
June 21 2007
Accepted Manuscript online:
June 21 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem J (2007) 406 (3): 399–406.
Article history
Received:
February 19 2007
Revision Received:
June 20 2007
Accepted:
June 21 2007
Accepted Manuscript online:
June 21 2007
Citation
Mark A. Hooks, James E. Turner, Elaine C. Murphy, Katherine A. Johnston, Sally Burr, Szymon Jarosławski; The Arabidopsis ALDP protein homologue COMATOSE is instrumental in peroxisomal acetate metabolism. Biochem J 15 September 2007; 406 (3): 399–406. doi: https://doi.org/10.1042/BJ20070258
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