We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase ofStreptococcus pneumoniaeand identification of kinase substrates.
- Authors
Nováková, Linda; Sasková, Lenka; Pallová, Petra; Janeček, Jiří; Novotná, Jana; Ulrych, Aleš; Echenique, Jose; Trombe, Marie-Claude; Branny, Pavel
- Abstract
Searching the genome sequence ofStreptococcus pneumoniaerevealed the presence of a single Ser/Thr protein kinase genestkPlinked to protein phosphatasephpP. Biochemical studies performed with recombinant StkP suggest that this protein is a functional eukaryotic-type Ser/Thr protein kinase.In vitrokinase assays and Western blots ofS. pneumoniaesubcellular fractions revealed that StkP is a membrane protein. PhpP is a soluble protein with manganese-dependent phosphatase activityin vitroagainst a synthetic substrate RRA(pT)VA. Mutations in the invariant aspartate residues implicated in the metal binding completely abolished PhpP activity. Autophosphorylated form of StkP was shown to be a substrate for PhpP. These results suggest that StkP and PhpP could operate as a functional pairin vivo. Analysis of phosphoproteome maps of both wild-type andstkPnull mutant strains labeledin vivoand subsequent phosphoprotein identification by peptide mass fingerprinting revealed two possible substrates for StkP. The evidence is presented that StkP can phosphorylatein vitrophosphoglucosamine mutase GlmM which catalyzes the first step in the biosynthetic pathway leading to the formation of UDP-N-acetylglucosamine, an essential common precursor to cell envelope components.
- Subjects
SERINE; AMINO acids; PROTEIN kinases; STREPTOCOCCUS pneumoniae; GENES; MEMBRANE proteins
- Publication
FEBS Journal, 2005, Vol 272, Issue 5, p1243
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04560.x