ZFIN ID: ZDB-PUB-170214-169
Crystal structure and potential physiological role of zebra fish thioesterase superfamily member 2 (fTHEM2)
Yu, S., Li, H., Gao, F., Zhou, Y.
Date: 2015
Source: Biochemical and Biophysical Research Communications   463: 912-6 (Journal)
Registered Authors:
Keywords: Early development of embryo, Morpholino, THEM2, Thioesterase, X-ray crystal structure, Zebra fish
MeSH Terms:
  • Animals
  • Base Sequence
  • Catalytic Domain
  • Crystallography, X-Ray
  • DNA Primers
  • Gene Knockdown Techniques
  • Palmitoyl-CoA Hydrolase/chemistry*
  • Palmitoyl-CoA Hydrolase/genetics
  • Palmitoyl-CoA Hydrolase/physiology*
  • Polymerase Chain Reaction
  • Protein Conformation
  • Zebrafish/embryology
  • Zebrafish Proteins/chemistry*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/physiology*
PubMed: 26067557 Full text @ Biochem. Biophys. Res. Commun.
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ABSTRACT
Thioesterase superfamily member 2 (THEM2) is an essential protein for mammalian cell proliferation. It belongs to the hotdog-fold thioesterase superfamily and catalyzes hydrolysis of thioester bonds of acyl-CoA in vitro, while its in vivo function remains unrevealed. In this study, Zebra fish was selected as a model organism to facilitate the investigations on THEM2. First, we solved the crystal structure of recombinant fTHEM2 at the resolution of 1.80 Å, which displayed a similar scaffolding as hTHEM2. Second, functional studies demonstrated that fTHEM2 is capable of hydrolyzing palmitoyl-CoA in vitro. In addition, injection of morpholino against fTHEM2 at one-cell stage resulted in distorted early embryo development, including delayed cell division, retarded development and increased death rate. The above findings validated our hypothesis that fTHEM2 could serve as an ideal surrogate for studying the physiological functions of THEM2.
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