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A eukaryotic-type serine/threonine protein kinase StkP ofStreptococcus pneumoniaeacts as a dimerin vivo

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
355
Issue
2
Identifiers
DOI: 10.1016/j.bbrc.2007.01.184
Keywords
  • Autophosphorylation
  • Dimerization
  • Serine/Threonine Protein Kinase
  • Streptococcus Pneumoniae
  • Signal Transduction
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract 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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