A eukaryotic-type serine/threonine protein kinase StkP of Streptococcus pneumoniae acts as a dimer in vivo.
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.
Pallová
Petra
P
Cell and Molecular Microbiology Division, Institute of Microbiology, Czech Academy of Sciences, Vídenská 1083, 142 20 Prague 4, Czech Republic.
Hercík
Kamil
K
Sasková
Lenka
L
Nováková
Linda
L
Branny
Pavel
P
D001426:Bacterial Proteins / Q000378:metabolism*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015398:Signal Transduction; D013296:Streptococcus pneumoniae / Q000201:enzymology*
D001426:Bacterial Proteins; D000939:Epitopes; D017346:Protein Serine-Threonine Kinases