creators_name: Pratap, J
creators_name: Kaur, J
creators_name: Rajamohan, Govindan
creators_name: Singh, Dawinder
creators_name: Dikshit, Kanak L
type: article
datestamp: 2011-12-16 08:56:41
lastmod: 2015-01-07 06:49:44
metadata_visibility: show
title: Role of N-terminal domain of streptokinase in protein transport.
ispublished: pub
subjects: QR
full_text_status: restricted
keywords: plasminogen; plasminogen activation mechanism; site-specific mutagenesis; streptokinase; substrate
plasminogen
note: Copyright of this article belongs to Wiley
abstract: Streptokinase (SK), an extracellular protein of several haemolytic strains of Streptococcus, is utilized as a potent thrombolytic agent for the treatment of various myocardial disorders. Functional properties of SK remain unchanged when the first 13 N-terminal amino acid (aa) residues are removed. At present, role of this segment in protein structure function is unclear. skc gene encoding for the mature SK and its deletion variant, lacking its first 13 aa residues, were cloned and expressed in E. coli. Full length SK, deprived of any leader sequences, was able to translocate slowly, across the cyto-plasmic and outer membranes of E.coli. Whereas, SK derivative, devoid of its first 13 N-terminal aa residues, could not do so. Cell fractionation studies as well as genetic evidences utilizing alkaline phosphatase fusion, point towards the existence of additional information for protein transport, within the N-terminal domain of SK. To further investigate the role of this region in protein secretion, genetic fusions were created in between full length and 13 aa deleted SK with OmpA leader peptide. Studies on kinetics of SK export from E.coli, revealed that translocation of protein is 3-4 times faster when the first 13 N-terminal residues of SK are intact. On the basis of results obtained, it has been proposed that the N-terminus of mature SK maintains the export competent status of protein and, thus, confer speed and efficiency upon the translocation process of streptokinase.
date: 1996-10-03
date_type: published
publication: Biochemical and biophysical research communications
volume: 227
number: 1
publisher: Wiley
pagerange: 303-10
refereed: TRUE
issn: 0006-291X
official_url: http://onlinelibrary.wiley.com/doi/10.1110/ps.8.12.2791/pdf
related_url_url: http://onlinelibrary.wiley.com/doi/10.1110/ps.8.12.2791/pdf
related_url_type: pub
citation:   Pratap, J and Kaur, J and Rajamohan, Govindan and Singh, Dawinder and Dikshit, Kanak L  (1996) Role of N-terminal domain of streptokinase in protein transport.  Biochemical and biophysical research communications, 227 (1).  pp. 303-10.  ISSN 0006-291X     
document_url: http://crdd.osdd.net/open/376/1/dawinder1999.pdf