Document Detail


An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: gene cloning, expression and characterization.
MedLine Citation:
PMID:  16896523     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A gene encoding an extracellular protease, sptA, was cloned from the halophilic archaeon Natrinema sp. J7. It encoded a polypeptide of 565 amino acids containing a putative 49-amino acid signal peptide, a 103-amino acid propeptide, as well as a mature region and C-terminal extension, with a high proportion of acidic amino acid residues. The sptA gene was expressed in Haloferax volcanii WFD11, and the recombinant enzyme could be secreted into the medium as an active mature form. The N-terminal amino acid sequencing and MALDI-TOF mass spectrometry analysis of the purified SptA protease indicated that the 152-amino acid prepropeptide was cleaved and the C-terminal extension was not processed after secretion. The SptA protease was optimally active at 50 degrees C in 2.5 M NaCl at pH 8.0. The NaCl removed enzyme retained 20% of its activity, and 60% of the activity could be restored by reintroducing 2.5 M NaCl into the NaCl removed enzyme. When the twin-arginine motif in the signal peptide of SptA protease was replaced with a twin-lysine motif, the enzyme was not exported from Hfx. volcanii WFD11, suggesting that the SptA protease was a Tat-dependent substrate.
Authors:
Wanliang Shi; Xiao-Feng Tang; Yuping Huang; Fei Gan; Bing Tang; Ping Shen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-07-29
Journal Detail:
Title:  Extremophiles : life under extreme conditions     Volume:  10     ISSN:  1431-0651     ISO Abbreviation:  Extremophiles     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2006-11-19     Completed Date:  2007-07-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9706854     Medline TA:  Extremophiles     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  599-606     Citation Subset:  IM; S    
Affiliation:
College of Life Sciences, Wuhan University, Wuhan 430072, People's Republic of China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Archaeal Proteins / chemistry*,  genetics,  metabolism
Caseins / metabolism
Cloning, Molecular*
Enzyme Stability
Halobacterium salinarum / enzymology*,  genetics
Haloferax volcanii / genetics,  metabolism
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Peptide Hydrolases / chemistry*,  genetics,  metabolism
Protein Processing, Post-Translational*
Protein Sorting Signals
Recombinant Proteins / chemistry
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Sodium Chloride / metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Temperature
Chemical
Reg. No./Substance:
0/Archaeal Proteins; 0/Caseins; 0/Protein Sorting Signals; 0/Recombinant Proteins; 0/azocasein; 7647-14-5/Sodium Chloride; EC 3.4.-/Peptide Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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