A eukaryotic-type serine/threonine protein kinase StkP of Streptococcus pneumoniae acts as a dimer in vivo
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17307148
DOI
10.1016/j.bbrc.2007.01.184
PII: S0006-291X(07)00268-9
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins metabolism MeSH
- Dimerization MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Epitopes metabolism MeSH
- Phosphorylation MeSH
- Protein Serine-Threonine Kinases metabolism MeSH
- Signal Transduction MeSH
- Streptococcus pneumoniae enzymology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Epitopes MeSH
- Protein Serine-Threonine Kinases MeSH
Streptococcus pneumoniae carries a single Ser/Thr protein kinase gene stkP in its genome. Biochemical studies performed with recombinant StkP have revealed that this protein is a functional membrane-linked eukaryotic-type Ser/Thr protein kinase. Here, we demonstrate that the deletion of its extracellular domain negatively affects the stability of a core kinase domain. In contrast, the membrane anchored kinase domain and the full-length form of StkP were stable and capable of autophosphorylation. Furthermore, evidence is presented that StkP forms dimers through its transmembrane and extracellular domains.
References provided by Crossref.org
GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division
General and molecular microbiology and microbial genetics in the IM CAS
Identification of multiple substrates of the StkP Ser/Thr protein kinase in Streptococcus pneumoniae
