Molecular Cloning and Sequencing of the Gene for a Halophilic Alkaline Serine Protease (halolysin) from an Unidentified Halophilic Archaea Strain (172P1) and Expression of the Gene in Haloferax Volcanii

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1992 Feb 1

PMID 1732209

Citations 30

Authors

M Kamekura

Y Seno

M L Holmes

M L Dyall-Smith

Affiliations

Soon will be listed here.

Abstract

The gene of a halophilic alkaline serine protease, halolysin, from an unidentified halophilic archaea (archaebacterium) was cloned and its nucleotide sequence was determined. The deduced amino acid sequence showed that halolysin consists of 411 amino acids, with a molecular weight of 41,963. The highest homology was found with thermitase from Thermoactinomyces vulgaris. Halolysin has a long C-terminal extension of approximately 120 amino acids which has not been found in other extracellular subtilisin type serine proteases. The gene, hly, was expressed in another halophilic archaea, Haloferax volcanii, in a medium containing 18% salts by using a plasmid shuttle vector which has a novobiocin resistance determinant as a selectable marker.

Citing Articles

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Hao Y, Jin Y, Zhang A, Jiang X, Gong M, Lu C World J Microbiol Biotechnol. 2024; 40(11):340.

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A TrmBL2-like transcription factor mediates the growth phase-dependent expression of halolysin SptA in a concentration-dependent manner in J7-2.

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Extracellular proteases from halophiles: diversity and application challenges.

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Hly176B, a low-salt tolerant halolysin from the haloarchaeon Haloarchaeobius sp. FL176.

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A novel halolysin without C-terminal extension from an extremely halophilic archaeon.

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