dc.contributor.author |
Griffith, O. H. |
|
dc.contributor.author |
McMillen, Debra A. |
|
dc.contributor.author |
Evans, Loreene M. |
|
dc.contributor.author |
Kuppe, Andreas |
|
dc.date.accessioned |
2017-02-08T23:18:53Z |
|
dc.date.available |
2017-02-08T23:18:53Z |
|
dc.date.issued |
1989-11 |
|
dc.identifier.uri |
http://hdl.handle.net/1794/22164 |
|
dc.description |
14 pages |
en_US |
dc.description.abstract |
The phosphatidylinositol (Pl)-specific phospholipase C (PLC) of Bacillus cereuswas cloned into Escherichia
coli by using monoclonal antibody probes raised against the purified protein. The enzyme is specific for
hydrolysis of the membrane lipid PI and Pl-glycan-containing membrane anchors, which are important
structural componentsof one class of membrane proteins. The protein expressedin E. colicomigrated with B.
cereus PI-PLC in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, as detected by immunoblotting,
and conferred PI-PLC activity on the host. This enzyme activity was inhibited by PI-PLC-specific monoclonal
antibodies. The nucleotide sequence of the PI-PLC gene suggests that this secreted bacterial protein is
synthesized as a larger precursor with a 31-amino-acid N-terminal extension to the mature enzyme of 298
amino acids. From analysis of coding and flanking sequences of the gene, weconclude that the PI-PLC gene
does not reside next to the gene cluster of the other two secreted phospholipases C on the bacterial chromosome.
The deduced amino acid sequence of the B. cereus PI-PLC contains a stretch of significant similarity to the
glycosylphosphatidylinositol-specific PLCof Trypanosoma brucei. The conserved peptide is proposed to playa
role in the function of these enzymes. |
en_US |
dc.publisher |
Journal of Bacteriology |
en_US |
dc.rights |
Creative Commons BY-NC-ND 4.0-US |
en_US |
dc.title |
Phosphatidylinositol-Specific Phospholipase C of Bacillus cereus: Cloning, Sequencing, and Relationship to Other Phospholipases |
en_US |
dc.type |
Article |
en_US |