The role of Spr1851 protein Streptococcus pneumoniae in cell division Human extracellular pathogen S. pneumoniae encodes unique serin/threonine protein kinase of Eucaryotic type StkP and its cognate phosphatase PhpP. This kinase affects number of cellular processes including virulence, competence, cell division and cell wall synthesis by phosphorylating its substrates. Hypothetical protein Spr1851 named Jag was identified as a new StkP substrate in the membrane fraction by comparing the wild-type phosphoproteomes with StkP deleted strain. This protein consists of three domains and an interdomain region that contains T89 phosphorylation site. There is a Jag_N domain with an unknown function at the N-terminus. The C-terminus contains two domains - KH and R3H, which are highly conserved and their expected function is binding of nucleic acid. The main aim of this work is to explain the function of Jag protein, to determine the effect of individual domains on the phenotype and the localization of the protein and to determine the role of phosphorylation on T89. The results confirm that Jag protein could play a role in cell division or cell wall synthesis. Furthermore, the results indicate that the Jag_N domain is essential for the localization of the protein into the membrane, whereas the KH and R3H domains are...
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:368405 |
| Date | January 2017 |
| Creators | Jarošová, Václava |
| Contributors | Ulrych, Aleš, Seydlová, Gabriela |
| Source Sets | Czech ETDs |
| Language | Czech |
| Detected Language | English |
| Type | info:eu-repo/semantics/masterThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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