Cytosolic ascorbate peroxidase 1 (APX1) plays a crucial role in regulating the level of plant cellular reactive oxygen species and its thermolability is proposed to cause plant heat-susceptibility. Herein, several hyper-acidic fusion partners, such as the C-terminal peptide tails, were evaluated for their effects on the thermal stability and activity of APX1 from Jatropha curcas and Arabidopsis. The hyper-acidic fusion partners efficiently improved the thermostability and prevented thermal inactivation of APX1 in both plant species with an elevated heat tolerance of at least 2 °C. These hyper-acidified thermostable APX1 fusion variants are of considerable biotechnological potential and can provide a new route to enhance the heat tolerance of plant species especially of inherent thermo-sensitivity.
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http://dx.doi.org/10.1007/s10529-014-1754-4 | DOI Listing |
Mol Ther Nucleic Acids
March 2023
Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Kunming, Yunnan 650500, China.
Methamphetamine (MA) is spread worldwide and is a highly addictive psychostimulant that can induce neurodegeneration and cognitive disorder, which lacks effective treatments. We and other researchers have found that the crucial member of Hsp70 chaperone machinery, DnaJ, is liable to be co-aggregated with aberrant proteins, which has been confirmed a risk factor to promote neurodegeneration. In the current study, we demonstrated that tailing with a hyper-acidic fusion partner, tua2, human DnaJB1 could resist the formation of toxic mutant Tau aggregates both in prokaryote and eukaryote models.
View Article and Find Full Text PDFJ Biotechnol
November 2021
Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming 650500, China. Electronic address:
The chaperone network plays an essential role in cellular protein homeostasis. However, some core components often coaggregate with misfolded proteins for sequestration and dysfunction, leading to abnormal cell proteostasis, aggregation-associated disorders, and poor solubility of overexpressed recombinant proteins. Among them, DnaJ or its ortholog, an obligate co-chaperone in the tripartite DnaK-DnaJ-GrpE system, is of more implications, probably due to its intrinsic propensity for aggregation.
View Article and Find Full Text PDFSci Rep
February 2019
Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, China.
C-reactive protein (CRP) is widely used as a biomarker of inflammation. It plays important roles in innate immunity response as a member of pattern recognition receptors, by binding oxidation-specific epitopes including some intermediates of lipid oxidative chain reaction. The inferred antioxidative ability of CRP was ever demonstrated by only few in vitro evidences, and needs to be clarified especially in vivo.
View Article and Find Full Text PDFJ Biotechnol
October 2015
School of Life Sciences, Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Key Laboratory of Biomass Energy and Environmental Biotechnology of Yunnan Province, Yunnan Normal University, Kunming 650500, Yunnan, China. Electronic address:
Thermostable fusion peptide partners are valuable in engineering thermostability in proteins. We evaluated the Arabidopsis counterpart (AtRAce) and an acidified derivative (mRAce) of the conserved carboxyl extension (RAce) of plant Rubisco activase (RCA) for their thermostabilizing properties in Escherichia coli and Saccharomyces cerevisiae using a protein fusion strategy. We used AtRAce and mRAce as fusion tails for the thermolabile protein RCA2 from Arabidopsis thaliana and Nicotiana tabacum.
View Article and Find Full Text PDFBiotechnol Lett
April 2015
Key Laboratory of Biomass Energy and Environmental Biotechnology of Yunnan Province, Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, Yunnan, China,
Cytosolic ascorbate peroxidase 1 (APX1) plays a crucial role in regulating the level of plant cellular reactive oxygen species and its thermolability is proposed to cause plant heat-susceptibility. Herein, several hyper-acidic fusion partners, such as the C-terminal peptide tails, were evaluated for their effects on the thermal stability and activity of APX1 from Jatropha curcas and Arabidopsis. The hyper-acidic fusion partners efficiently improved the thermostability and prevented thermal inactivation of APX1 in both plant species with an elevated heat tolerance of at least 2 °C.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!