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A eukaryotic-type serine/threonine protein kinase StkP of Streptococcus pneumoniae acts as a dimer in vivo
Pallová P, Hercík K, Sasková L, Nováková L, Branny P
Jazyk angličtina Země Spojené státy americké
NLK
ScienceDirect (archiv)
od 1993-01-01 do 2009-12-31
- MeSH
- bakteriální proteiny metabolismus MeSH
- dimerizace MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- epitopy metabolismus MeSH
- financování organizované MeSH
- fosforylace MeSH
- protein-serin-threoninkinasy metabolismus MeSH
- signální transdukce MeSH
- Streptococcus pneumoniae enzymologie 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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- $a 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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