TAILIEUCHUNG - Báo cáo khoa học: Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates

Searching the genome sequence ofStreptococcus pneumoniaerevealed the presence of a single Ser⁄Thr protein kinase genestkP linked to protein phosphatasephpP. Biochemical studies performed with recombinant StkP suggest that this protein is a functional eukaryotic-type Ser⁄Thr protein vitrokinase assays and Western blots ofS. pneumoniaesubcellu-lar fractions revealed that StkP is a membrane protein. | ềFEBS Journal Characterization of a eukaryotic type serine threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates Linda Nováková1 Lenka Saskova1 Petra Pallova1 Jiri Janecek1 Jana Novotna1 Ales Ulrych1 Jose Echenique2 Marie-Claude Trombe3 and Pavel Branny1 1 Celland Molecular Microbiology Division Institute of Microbiology Czech Academy of Sciences Prague Czech Republic 2 Departamento de Bioquimica Clinica Facultad de Ciencias Quimicas Universidad Nacionalde Cordoba Medina Allende esq Haya de la Torre Ciudad Universitaria Cordoba Argentina 3 Centre Hospitalo-Universitaire de Rangueil Universite PaulSabatier Toulouse France Keywords phosphoglucosamine mutase phosphoproteome protein phosphatase serine threonine protein kinase Streptococcus pneumoniae Correspondence P. Branny Celland Molecular Microbiology Division Institute of Microbiology Czech Academy of Sciences Vídeiăská 1083 142 20 Prague 4 Czech Republic Fax 420 2 41722257 Tel 420 2 41062658 E-mail branny@ Received 25 August 2004 revised 21 December 2004 accepted 7 January 2005 doi Searching the genome sequence of Streptococcus pneumoniae revealed the presence of a single Ser Thr protein kinase gene stkP linked to protein phosphatase phpP. Biochemical studies performed with recombinant StkP suggest that this protein is a functional eukaryotic-type Ser Thr protein kinase. In vitro kinase assays and Western blots of S. pneumoniae subcellu-lar fractions revealed that StkP is a membrane protein. PhpP is a soluble protein with manganese-dependent phosphatase activity in vitro against 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 pair in vivo. Analysis of phosphoproteome .

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