Autocatalytic maturation of the Tat-dependent halophilic subtilase Nep produced by the archaeon Natrialba magadii.

Journal of Bacteriology
D M RuizR E De Castro

Abstract

Halolysins are subtilisin-like extracellular proteases produced by haloarchaea that possess unique protein domains and are salt dependent for structural integrity and functionality. In contrast to bacterial subtilases, the maturation mechanism of halolysins has not been addressed. The halolysin Nep is secreted by the alkaliphilic haloarchaeon Natrialba magadii, and the recombinant active enzyme has been synthesized in Haloferax volcanii. Nep contains an N-terminal signal peptide with the typical Tat consensus motif (GRRSVL), an N-terminal propeptide, the protease domain, and a C-terminal domain. In this study, we used Nep as a model protease to examine the secretion and maturation of halolysins by using genetic and biochemical approaches. Mutant variants of Nep were constructed by site-directed mutagenesis and expressed in H. volcanii, which were then analyzed by protease activity and Western blotting. The Tat dependence of Nep secretion was demonstrated in Nep RR/KK variants containing double lysine (KK) in place of the twin arginines (RR), in which Nep remained cell associated and the extracellular activity was undetectable. High-molecular-mass Nep polypeptides without protease activity were detected as cell associated and ex...Continue Reading

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Citations

Feb 12, 2014·Journal of Proteome Research·Jie FengXiao-Feng Tang
Jul 9, 2014·Applied and Environmental Microbiology·Yaoxin ZhangXiao-Feng Tang
Dec 1, 2018·Emerging Topics in Life Sciences·Julie A Maupin-Furlow
Feb 14, 2021·Applied and Environmental Microbiology·Shaoxing ChenHua Xiang

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