Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch
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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 Elo; Dyer, James H; Arent, Susan; Henriksen, Anette.
In: The Journal of Biological Chemistry, Vol. 285, No. 31, 30.07.2010, p. 24078-88.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch
AU - Pye, Valerie E
AU - Christensen, Caspar Elo
AU - Dyer, James H
AU - Arent, Susan
AU - Henriksen, Anette
PY - 2010/7/30
Y1 - 2010/7/30
N2 - The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-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 A 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 beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.
AB - The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-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 A 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 beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.
KW - Acetyl-CoA C-Acyltransferase
KW - Arabidopsis
KW - Cloning, Molecular
KW - Crystallography, X-Ray
KW - Dimerization
KW - Fatty Acids
KW - Gene Expression Regulation, Enzymologic
KW - Gene Expression Regulation, Plant
KW - Helianthus
KW - Lipids
KW - Models, Biological
KW - Oxidation-Reduction
KW - Oxygen
KW - Peroxisomes
KW - Substrate Specificity
U2 - 10.1074/jbc.M110.106013
DO - 10.1074/jbc.M110.106013
M3 - Journal article
C2 - 20463027
VL - 285
SP - 24078
EP - 24088
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 31
ER -
ID: 104026263