Anti-Tumor Effects of a Newly Cloned Serine Protease from the Marine Annelid, Arenicola cristata

We cloned a new serine protease gene from the marine annelid,Arenicola cristataby rapid amplification of cDNA ends. The full-length cDNA of 901bp contained an open reading frame of 774bp encoding 258 amino acids. Sequence analysis of the deduced amino acids indicated that this protease belonged to serine protease family and contained highly conserved sequence GDSGGP. An expression vector, harboring the mature peptide ofArenicola cristataprotease, was constructed and transformed intoE.coli. The purified recombinant protein could inhibit proliferation of cancer cells in a dose-dependant way and induce apoptosis. These results indicated that the recombinant protease ofArenicola cristata, as a new member of serine protease family, might be valuable in developing anti-tumor agents.

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The Protein Encoded at the 3′ End of the Serine Protease Gene of Aeromonas sobria Functions as a Chaperone in the Production of the Protease

Journal of Bacteriology ◽

10.1128/jb.184.24.7058-7061.2002 ◽

2002 ◽

Vol 184 (24) ◽

pp. 7058-7061 ◽

Cited By ~ 9

Author(s):

Tomohiko Nomura ◽

Yoshio Fujii ◽

Hiroyasu Yamanaka ◽

Hidetomo Kobayashi ◽

Keinosuke Okamoto

Keyword(s):

Serine Protease ◽

Open Reading Frame ◽

Protease Gene ◽

Reading Frame ◽

Active Structure ◽

Aeromonas Sobria ◽

Orf2 Protein ◽

Open Reading Frame 2 ◽

Serine Protease Gene ◽

Successful Production

ABSTRACT For the successful production of Aeromonas sobria serine protease (ASP), open reading frame 2 (ORF2) protein, encoded at the 3′ end of the protease operon, is required. In this study, we examined the action of ORF2 protein. The results showed that the protein associated with ASP in the periplasm and helped ASP to form an active structure.

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Cloning of a serine protease gene from the nematophagous fungus Esteya vermicola and expressed activity of the recombinant enzyme against Bursaphelenchus xylophilus

Nematology ◽

10.1163/15685411-00002924 ◽

2015 ◽

Vol 17 (9) ◽

pp. 1071-1080 ◽

Cited By ~ 1

Author(s):

Xuan Wang ◽

Tinglong Guan ◽

Long Zhang ◽

Hongmei Li

Keyword(s):

Amino Acids ◽

Serine Protease ◽

Phylogenetic Analyses ◽

Bursaphelenchus Xylophilus ◽

Nematophagous Fungus ◽

Infection Process ◽

Fungal Genome ◽

Protease Gene ◽

Esteya Vermicola ◽

Serine Protease Gene

A serine protease geneEvspwas cloned from the nematophagous fungusEsteya vermicolawith strong virulence againstBursaphelenchus xylophilus. The full-length cDNA ofEvspcontains 2280 nucleotides with a 1656 bp ORF encoding a protein with 551 amino acids. The genomicEvspincludes two exons (396 bp and 1260 bp) separated by an intron (207 bp). There is only one copy ofEvspgene in the fungal genome. The deduced amino acids sequences ofEvspshowed highly homology with the catalytic domains in subtilisin serine proteases. Phylogenetic analyses based on the protein sequences revealed thatE. vermicolais separated from nematode-trapping fungi but close to other nematophagous and entomopathogenic fungi. The recombinant serine protease rEvsp was induced inEscherichia coliwith expression vector pET28a(+). The tests of protease and nematicidal activities for the purified and refolded rEvsp indicated it is possibly involved in the fungal infection process againstB. xylophilus.

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