A eukaryotic-type serine/threonine protein kinase StkP of Streptococcus pneumoniae acts as a dimer in vivo
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
17307148
DOI
10.1016/j.bbrc.2007.01.184
PII: S0006-291X(07)00268-9
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny metabolismus MeSH
- dimerizace MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- epitopy metabolismus MeSH
- fosforylace MeSH
- protein-serin-threoninkinasy metabolismus MeSH
- signální transdukce MeSH
- Streptococcus pneumoniae enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- epitopy MeSH
- protein-serin-threoninkinasy 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.
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