Open AccessPauA: a novel plasminogen activator from Streptococcus uberis
Author(s) -
Rosey E.L.,
Lincoln R.A.,
Ward P.N.,
Yancey R.J.,
Leigh J.A.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13755.x
Subject(s) - biology , streptococcus uberis , microbiology and biotechnology , nucleic acid sequence , gene , streptococcus gordonii , activator (genetics) , peptide sequence , biochemistry , streptococcaceae , genetics , streptococcus , bacteria , antibiotics
Chromosomal DNA from two geographically distinct isolates of Streptococcus uberis was used to clone the plasminogen activator in an active form in Escherichia coli . The cloned fragments from each strain contained four potential open reading frames (ORFs). That for the plasminogen activator encoded a protein of 286 amino acids (33.4 kDa) which is cleaved between residues 25 and 26 during secretion by S. uberis . The amino acid sequence of the mature protein showed only weak homology (23.5–28%) to streptokinase. The plasminogen activator gene, pauA , in S. uberis was located between two ORFs with high homology to the DNA mismatch repair genes, hexA and hexB , and not on a DNA fragment between the genes encoding an ATP binding cassette transporter protein ( abc ) and a protein involved in the formation and degradation of guanosine polyphosphates ( rel ) as is the case for streptokinase in other streptococci.