Počet záznamů: 1
Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag
- 1.
SYSNO ASEP 0465661 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag Tvůrce(i) Ulrych, Aleš (MBU-M) RID
Holečková, Nela (MBU-M)
Goldová, Jana (MBU-M) RID
Doubravová, Linda (MBU-M) ORCID, RID
Benada, Oldřich (MBU-M) ORCID, RID
Kofroňová, Olga (MBU-M) RID, ORCID
Halada, Petr (MBU-M) RID, ORCID
Branny, Pavel (MBU-M) RID, ORCIDZdroj.dok. BMC Microbiology. - : BioMed Central - ISSN 1471-2180
Roč. 16, OCT 24 (2016), s. 247Poč.str. 19 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Signal transduction ; Protein phosphatase ; Protein kinase Vědní obor RIV EE - Mikrobiologie, virologie CEP GAP302/12/0256 GA ČR - Grantová agentura ČR GAP207/12/1568 GA ČR - Grantová agentura ČR LH12055 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora MBU-M - RVO:61388971 UT WOS 000385973900001 EID SCOPUS 84992186990 DOI https://doi.org/10.1186/s12866-016-0865-6 Anotace Background: Reversible protein phosphorylation catalyzed by protein kinases and phosphatases is the primary mechanism for signal transduction in all living organisms. Streptococcus pneumoniae encodes a single Ser/Thr protein kinase, StkP, which plays a role in virulence, stress resistance and the regulation of cell wall synthesis and cell division. However, the role of its cognate phosphatase, PhpP, is not well defined.
Results: Here, we report the successful construction of Delta phpP mutant in the unencapsulated S. pneumoniae Rx1 strain and the characterization of its phenotype. We demonstrate that PhpP negatively controls the level of protein phosphorylation in S. pneumoniae both by direct dephosphorylation of target proteins and by dephosphorylation of its cognate kinase, StkP. Catalytic inactivation or absence of PhpP resulted in the hyperphosphorylation of StkP substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the Delta phpP cells resembled the StkP overexpression phenotype and conversely, overexpression of PhpP resulted in cell elongation mimicking the stkP null phenotype. Proteomic analysis of the phpP knock-out strain permitted identification of a novel StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Here, we show that pneumococcal Jag is phosphorylated on Thr89. Inactivation of jag confers a phenotype similar to the phpP mutant strain.
Conclusions: Our results suggest that PhpP and StkP cooperatively regulate cell division of S. pneumoniae and phosphorylate putative RNA binding protein Jag.Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2017
Počet záznamů: 1