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

被引：25

作者：

Pallova, Petra ^{[1
]}

Hercik, Kamil ^{[1
]}

Saskova, Lenka ^{[1
]}

Novakova, Linda ^{[1
]}

Branny, Pavel ^{[1
]}

机构：

[1] Acad Sci Czech Republ, Inst Microbiol, Cell & Mol Microbiol Div, Prague 14220 4, Czech Republic

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 355卷 / 02期

关键词：

autophosphorylation; dimerization; serine/threonine protein kinase; Streptococcus pneumoniae; signal transduction;

D O I：

10.1016/j.bbrc.2007.01.184

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：526 / 530

页数：5