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Biochem Biophys Res Commun. 2007 Apr 6;355(2):526-30. Epub 2007 Feb 8.

A eukaryotic-type serine/threonine protein kinase StkP of Streptococcus pneumoniae acts as a dimer in vivo.

Author information

1
Cell and Molecular Microbiology Division, Institute of Microbiology, Czech Academy of Sciences, Vídenská 1083, 142 20 Prague 4, Czech Republic.

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.

PMID:
17307148
DOI:
10.1016/j.bbrc.2007.01.184
[Indexed for MEDLINE]

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