ArticleApplied and environmental microbiology2014
Chitin accelerates activation of a novel haloarchaeal serine protease that deproteinizes chitin-containing biomass.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- A haloarchaeal VapBC toxin-antitoxin system: regulatory mechanism and role in establishing population heterogeneity to facilitate survival of subpopulations under stress conditions.Applied and environmental microbiology · 2026Article
- Identification and characterization of a novel halolysin from Halostella sp. PRR32 with two C-terminal extensions.Extremophiles : life under extreme conditions · 2025Article
- Identification and biochemical characterization of a novel halolysin from Halorubellus sp. PRR65 with a relatively high temperature activity.World journal of microbiology & biotechnology · 2024Article
- A TrmBL2-like transcription factor mediates the growth phase-dependent expression of halolysin SptA in a concentration-dependent manner inApplied and environmental microbiology · 2024Article
- HtrAs are essential for the survival of the haloarchaeonApplied and environmental microbiology · 2024Article
- Expression, purification, and enzymatic characterization of an extracellular protease from Halococcus salifodinae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Extracellular proteases from halophiles: diversity and application challenges.Applied microbiology and biotechnology · 2023Review
- Recent advances in the production, properties and applications of haloextremozymes protease and lipase from haloarchaea.World journal of microbiology & biotechnology · 2023Review
- Dissecting the Arginine and Lysine Biosynthetic Pathways and Their Relationship in Haloarchaeon Natrinema gari J7-2 via Endogenous CRISPR-Cas System-Based Genome Editing.Microbiology spectrum · 2023Article
- Hly176B, a low-salt tolerant halolysin from the haloarchaeon Haloarchaeobius sp. FL176.World journal of microbiology & biotechnology · 2023Article
- Sec-Dependent Secretion of Subtilase SptE inApplied and environmental microbiology · 2022Article
- A novel halolysin without C-terminal extension from an extremely halophilic archaeon.Applied microbiology and biotechnology · 2022Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Halolysin SptA, a Serine Protease, Contributes to Growth-Phase Transition of HaloarchaeonFrontiers in microbiology · 2018Article
- Construction of Expression Shuttle Vectors for the HaloarchaeonArchaea (Vancouver, B.C.) · 2017Article
- Alternative Translation Initiation of a Haloarchaeal Serine Protease Transcript Containing Two In-Frame Start Codons.Journal of bacteriology · 2016Article
- Halophiles and their enzymes: negativity put to good use.Current opinion in microbiology · 2015Review
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Authors and funding
9 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The haloarchaeon Natrinema sp. strain J7-2 has the ability to degrade chitin, and its genome harbors a chitin metabolism-related gene cluster that contains a halolysin gene, sptC. The sptC gene encodes a precursor composed of a signal peptide, an N-terminal propeptide consisting of a core domain (N*) and a linker peptide, a subtilisin-like catalytic domain, a polycystic kidney disease domain (PkdD), and a chitin-binding domain (ChBD). Here we report that the autocatalytic maturation of SptC is initiated by cis-processing of N* to yield an autoprocessed complex (N*-I(WT)), followed by trans-processing/degradation of the linker peptide, the ChBD, and N*. The resulting mature form (M(WT)) containing the catalytic domain and the PkdD showed optimum azocaseinolytic activity at 3 to 3.5 M NaCl, demonstrating salt-dependent stability. Deletion analysis revealed that the PkdD did not confer extra stability on the enzyme but did contribute to enzymatic activity. The ChBD exhibited salt-dependent chitin-binding capacity and mediated the binding of N*-I(WT) to chitin. ChBD-mediated chitin binding enhances SptC maturation by promoting activation of the autoprocessed complex. Our results also demonstrate that SptC is capable of removing proteins from shrimp shell powder (SSP) at high salt concentrations. Interestingly, N*-I(WT) released soluble peptides from SSP faster than did M(WT). Most likely, ChBD-mediated binding of the autoprocessed complex to chitin in SSP not only accelerates enzyme activation but also facilitates the deproteinization process by increasing the local protease concentration around the substrate. By virtue of these properties, SptC is highly attractive for use in preparation of chitin from chitin-containing biomass.
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