Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase

Nature Communications
Fuyuan JingBasil J Nikolau

Abstract

The substrate specificity of acyl-ACP thioesterase (TE) plays an essential role in controlling the fatty acid profile produced by type II fatty acid synthases. Here we identify two groups of residues that synergistically determine different substrate specificities of two acyl-ACP TEs from Cuphea viscosissima (CvFatB1 and CvFatB2). One group (V194, V217, N223, R226, R227, and I268 in CvFatB2) is critical in determining the structure and depth of a hydrophobic cavity in the N-terminal hotdog domain that binds the substrate's acyl moiety. The other group (255-RKLSKI-260 and 285-RKLPKL-289 in CvFatB2) defines positively charged surface patches that may facilitate binding of the ACP moiety. Mutagenesis of residues within these two groups results in distinct synthetic acyl-ACP TEs that efficiently hydrolyze substrates with even shorter chains (C4- to C8-ACPs). These insights into structural determinants of acyl-ACP TE substrate specificity are useful in modifying this enzyme for tailored fatty acid production in engineered organisms.

References

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Citations

Oct 31, 2019·Annals of Botany·Chloé GuerinStéphane Dussert
Jan 15, 2021·Organic & Biomolecular Chemistry·Beatriz de Pina MarizAna Sofia Pina
Feb 28, 2021·Cellular and Molecular Life Sciences : CMLS·Ana Rita CavacoAndreia Figueiredo
Apr 19, 2020·Current Opinion in Plant Biology·Edgar B Cahoon, Yonghua Li-Beisson
Aug 29, 2020·Structure·Ratul ChowdhuryCostas D Maranas
Jul 29, 2021·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·Zhou ZhouKhalid Meksem
Aug 2, 2018·ACS Synthetic Biology·Néstor J Hernández LozadaBrian F Pfleger
Sep 7, 2021·Applied Microbiology and Biotechnology·Siti Hajar HamdanThean Chor Leow

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Datasets Mentioned

BETA
JF338906

Methods Mentioned

BETA
PCR
electrophoresis
Protein Assay

Software Mentioned

PyMOL Molecular Graphics System
2OWN
TASSER

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