New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution

Sunflower seeds ( L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity , the enzymes that terminate the process of fatty acid synthesis by catalyzing the hydrol...

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Vydáno v:Frontiers in plant science Ročník 9; s. 1496
Hlavní autoři: Aznar-Moreno, Jose A., Sánchez, Rosario, Gidda, Satinder K., Martínez-Force, Enrique, Moreno-Pérez, Antonio J., Venegas Calerón, Mónica, Garcés, Rafael, Mullen, Robert T., Salas, Joaquín J.
Médium: Journal Article
Jazyk:angličtina
Vydáno: Switzerland Frontiers Media SA 16.10.2018
Frontiers Media S.A
Témata:
Acyl carrier protein
acyl-ACP thioesterase
Amino acids
Biosynthesis
Chemical synthesis
Cloning
Crystal structure
Enzymes
FatA
FatB
Fatty acids
Fatty-acid synthase
Flowering
Flowers & plants
Fractionation
Helianthus annuus
Hydrophobicity
Plant Science
protein location
Proteins
Seeds
Stroma
sunflower
Sunflower oil
Thioesterase
Transmembrane domains
Triglycerides
Germany
FatB
FatA
acyl-ACP thioesterase
Helianthus annuus
protein location
sunflower
ISSN:1664-462X, 1664-462X
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Shrnutí:Sunflower seeds ( L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity , the enzymes that terminate the process of fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using imaging and organelle fractionation, thioesterases, FatA and FatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by FatA and FatB in oil biosynthesis are discussed in the light of our data.
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Reviewed by: Edgar B. Cahoon, University of Nebraska–Lincoln, United States; Kun Wang, Harvard T.H. Chan School of Public Health, United States
Edited by: Ján A. Miernyk, Agricultural Research Service (USDA), United States
This article was submitted to Plant Physiology, a section of the journal Frontiers in Plant Science
ISSN:1664-462X
1664-462X
DOI:10.3389/fpls.2018.01496