Novel self-cleavage activity of Staphylokinase fusion proteins: An interesting finding and its possible applications.

Abstract:

:Staphylokinase (SAK) is reported to have a serine protease domain with no proteolytic activity unlike other plasminogen activators like tissue plasminogen activator (t-PA) and urokinase. A unique protease property of Staphylokinase was observed when SAK was expressed as a fusion protein in inducible Escherichia coli expression vectors. This finding was further investigated by cloning and expressing different SAK fusions, both native and N-terminal deletions, with fusion tags like glutathione S-transferase (GST) and signal sequence of SAK in bacterial system. While all the N-terminal SAK fusions were found to self-cleave in crude and purified preparations, the C-terminal SAK fusion was stable. The cleavage property of Staphylokinase fusion proteins, inhibited by reduced glutathione and PMSF, was independent of its thrombolytic activity and also independent on the type of host employed for its expression. The serine protease domain of the SAK gene possibly lies between 20th to 77th amino acid and serine 41 of this region appears critical for such a cleavage property.

journal_name

Protein Expr Purif

authors

Prasad B,Salunkhe SS,Padmanabhan S

doi

10.1016/j.pep.2009.07.011

subject

Has Abstract

pub_date

2010-02-01 00:00:00

pages

191-7

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(09)00179-X

journal_volume

69

pub_type

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