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Int. J. Mol. Sci. 2017, 18(1), 113; doi:10.3390/ijms18010113

Pnserpin: A Novel Serine Protease Inhibitor from Extremophile Pyrobaculum neutrophilum

1
Department of Cell Biology, College of Basic Medical Sciences, Jilin University, Changchun 130021, China
2
State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China
3
Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun 130012, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Charles A. Collyer
Received: 10 August 2016 / Revised: 29 December 2016 / Accepted: 3 January 2017 / Published: 7 January 2017
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [3089 KB, uploaded 9 January 2017]   |  

Abstract

Serine protease inhibitors (serpins) are native inhibitors of serine proteases, constituting a large protein family with members spread over eukaryotes and prokaryotes. However, only very few prokaryotic serpins, especially from extremophiles, have been characterized to date. In this study, Pnserpin, a putative serine protease inhibitor from the thermophile Pyrobaculum neutrophilum, was overexpressed in Escherichia coli for purification and characterization. It irreversibly inhibits chymotrypsin-, trypsin-, elastase-, and subtilisin-like proteases in a temperature range from 20 to 100 °C in a concentration-dependent manner. The stoichiometry of inhibition (SI) of Pnserpin for proteases decreases as the temperature increases, indicating that the inhibitory activity of Pnserpin increases with the temperature. SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) showed that Pnserpin inhibits proteases by forming a SDS-resistant covalent complex. Homology modeling and molecular dynamic simulations predicted that Pnserpin can form a stable common serpin fold. Results of the present work will help in understanding the structural and functional characteristics of thermophilic serpin and will broaden the current knowledge about serpins from extremophiles. View Full-Text
Keywords: Pnserpin; serine protease inhibitor; thermophile Pnserpin; serine protease inhibitor; thermophile
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Zhang, H.; Fei, R.; Xue, B.; Yu, S.; Zhang, Z.; Zhong, S.; Gao, Y.; Zhou, X. Pnserpin: A Novel Serine Protease Inhibitor from Extremophile Pyrobaculum neutrophilum. Int. J. Mol. Sci. 2017, 18, 113.

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