Qiu T

References (3)

Title : ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5 - Cao_2019_Nat.Chem.Biol_15_1232
Author(s) : Cao Y , Qiu T , Kathayat RS , Azizi SA , Thorne AK , Ahn D , Fukata Y , Fukata M , Rice PA , Dickinson BC
Ref : Nat Chemical Biology , 15 :1232 , 2019
Abstract : S-Palmitoylation is a reversible lipid post-translational modification that has been observed on mitochondrial proteins, but both the regulation and functional consequences of mitochondrial S-palmitoylation are poorly understood. Here, we show that perturbing the 'erasers' of S-palmitoylation, acyl protein thioesterases (APTs), with either pan-active inhibitors or a mitochondrial-targeted APT inhibitor, diminishes the antioxidant buffering capacity of mitochondria. Surprisingly, this effect was not mediated by the only known mitochondrial APT, but rather by a resident mitochondrial protein with no known endogenous function, ABHD10. We show that ABHD10 is a member of the APT family of regulatory proteins and identify peroxiredoxin-5 (PRDX5), a key antioxidant protein, as a target of ABHD10 S-depalmitoylase activity. We then find that ABHD10 regulates the S-palmitoylation status of the nucleophilic active site residue of PRDX5, providing a direct mechanistic connection between ABHD10-mediated S-depalmitoylation of PRDX5 and its antioxidant capacity.
ESTHER : Cao_2019_Nat.Chem.Biol_15_1232
PubMedSearch : Cao_2019_Nat.Chem.Biol_15_1232
PubMedID: 31740833
Gene_locus related to this paper: human-ABHD10 , mouse-abhda

Title : A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells - Qiu_2018_Biochemistry_57_221
Author(s) : Qiu T , Kathayat RS , Cao Y , Beck MW , Dickinson BC
Ref : Biochemistry , 57 :221 , 2018
Abstract : S-Palmitoylation is an abundant lipid post-translational modification that is dynamically installed on and removed from target proteins to regulate their activity and cellular localization. A dearth of tools for studying the activities and regulation of protein S-depalmitoylases, thioesterase "erasers" of protein cysteine S-palmitoylation, has contributed to an incomplete understanding of the role of dynamic S-palmitoylation in regulating proteome lipidation. Recently, we developed "depalmitoylation probes" (DPPs), small molecule probes that become fluorescent upon S-depalmitoylase enzymatic activity. To be suitable for application in live cells, the first-generation DPPs relied on a shorter lipid substrate (C8 vs naturally occurring C16), which enhanced solubility and cell permeability. However, the use of an unnatural lipid substrate on the probes potentially limits the utility of the approach. Herein, we present a new member of the DPP family, DPP-5, which features an anionic carboxylate functional group that increases the probe water solubility. The enhanced water solubility of DPP-5 permits the use of a natural, palmitoylated substrate (C16), rather than a surrogate lipid. We show that DPP-5 is capable of monitoring endogenous S-depalmitoylases in live mammalian cells and that it can reveal changes in S-depalmitoylation levels due to lipid stress. DPP-5 should prove to be a useful new tool for probing the regulation of proteome lipidation through dynamic S-depalmitoylation.
ESTHER : Qiu_2018_Biochemistry_57_221
PubMedSearch : Qiu_2018_Biochemistry_57_221
PubMedID: 29023093

Title : Molecular Cloning and Characterization of a Novel Cold-Adapted Family VIII Esterase from a Biogas Slurry Metagenomic Library - Cheng_2014_J.Microbiol.Biotechnol_24_1484
Author(s) : Cheng X , Wang X , Qiu T , Yuan M , Sun J , Gao J
Ref : J Microbiol Biotechnol , 24 :1484 , 2014
Abstract : A novel esterase gene, est01, was successfully unearthed from a biogas digester microbiota metagenomic library. The 1,194 bp est01 gene encodes a protein of 44,804 Da (designated Est01). The amino acid sequence of Est01 shows only moderate (33%) identity to a lipase/ esterase. Phylogenetic analysis and biochemical characterization confirmed that Est01 is a new member of family VIII esterases. The purified Est01 from recombinant Escherichia coli BL21 (DE3) showed high hydrolytic activity against short-chain fatty acid esters, suggesting that it is a typical carboxylesterase rather than a lipase. Furthermore, the Est01 was even active at 10 degrees C (43% activity remained), with the optimal temperature at 20 degrees C, and had a broad pH range from 5.0 to 10.0, with the optimal pH of 8.0. These properties suggest that Est01 is a cold-adaptive esterase and could have good potential for low-temperature hydrolysis application.
ESTHER : Cheng_2014_J.Microbiol.Biotechnol_24_1484
PubMedSearch : Cheng_2014_J.Microbiol.Biotechnol_24_1484
PubMedID: 25394508