Highly conserved nucleotide phosphatase essential for membrane lipid homeostasis in Streptococcus pneumoniae.
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Authors
Kuipers, KirstenGallay, Clement
Martínek, Václav
Rohde, M
Martínková, Markéta
van der Beek, Samantha L
Jong, Wouter S P
Venselaar, Hanka
Zomer, Aldert
Bootsma, Hester
Veening, Jan-Willem
de Jonge, Marien I
Issue Date
2016-07
Metadata
Show full item recordAbstract
Proteins belonging to the DHH family, a member of the phosphoesterase superfamily, are produced by most bacterial species. While some of these proteins are well studied in Bacillus subtilis and Escherichia coli, their functions in Streptococcus pneumoniae remain unclear. Recently, the highly conserved DHH subfamily 1 protein PapP (SP1298) has been reported to play an important role in virulence. Here, we provide a plausible explanation for the attenuated virulence of the papP mutant. Recombinant PapP specifically hydrolyzed nucleotides 3'-phosphoadenosine-5'-phosphate (pAp) and 5'-phosphoadenylyl-(3'->5')-adenosine (pApA). Deletion of papP, potentially leading to pAp/pApA accumulation, resulted in morphological defects and mis-localization of several cell division proteins. Incubation with both polar solvent and detergent led to robust killing of the papP mutant, indicating that membrane integrity is strongly affected. This is in line with previous studies showing that pAp inhibits the ACP synthase, an essential enzyme involved in lipid precursor production. Remarkably, partial inactivation of the lipid biosynthesis pathway, by inhibition of FabF or depletion of FabH, phenocopied the papP mutant. We conclude that pAp and pApA phosphatase activity of PapP is required for maintenance of membrane lipid homeostasis providing an explanation how inactivation of this protein may attenuate pneumococcal virulence.Citation
Highly conserved nucleotide phosphatase essential for membrane lipid homeostasis in Streptococcus pneumoniae. 2016, 101 (1):12-26 Mol. Microbiol.Affiliation
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig.Journal
Molecular microbiologyPubMed ID
26691161Type
ArticleLanguage
enISSN
1365-2958ae974a485f413a2113503eed53cd6c53
10.1111/mmi.13312
Scopus Count
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- Creative Commons
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/