Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch

Valerie E. Pye, Caspar E. Christensen, Jim Dyer, Susan Arent, Anette Henriksen

Research output: Contribution to journalArticleResearchpeer-review

19 Citations (Scopus)

Abstract

The breakdown of fatty acids, performed by the β-oxidation cycle, is crucial for plant germination and sustainability. β-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 Å resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in β-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.

Original languageEnglish
Pages (from-to)24078-24088
Number of pages11
JournalJournal of Biological Chemistry
Volume285
Issue number31
DOIs
StatePublished - 30 Jul 2010

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Acetyl-CoA C-Acyltransferase
Oxidation-Reduction
Fatty Acids
Switches
Oxidation
Peroxisomes
Helianthus
Germination
Immunoprecipitation
Arabidopsis
Dimers
Conformations
Sustainable development
Catalytic Domain
Carbon
Crystal structure
Substrates
Proteins

Cite this

Pye, Valerie E. ; Christensen, Caspar E. ; Dyer, Jim ; Arent, Susan ; Henriksen, Anette. / Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 31. pp. 24078-24088.
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abstract = "The breakdown of fatty acids, performed by the β-oxidation cycle, is crucial for plant germination and sustainability. β-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 {\AA} resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in β-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.",
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Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch. / Pye, Valerie E.; Christensen, Caspar E.; Dyer, Jim; Arent, Susan; Henriksen, Anette.

In: Journal of Biological Chemistry, Vol. 285, No. 31, 30.07.2010, p. 24078-24088.

Research output: Contribution to journalArticleResearchpeer-review

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