Transcriptional regulon controlled by tyrosine phosphatases in Porphyromonas gingivalis

ABSTRACT: Tyrosine phosphorylation/dephosphorylation posttranslational modification (PTM) of proteins in bacteria can control their function and location. While PTM of transcriptional regulators and DNA-binding proteins impacts gene transcription, little is known regarding the transcriptional landscape regulating tyrosine phospho-relay circuitry. In this study, we performed RNA-Seq of Porphyromonas gingivalis strains with mutations in ltp1 and php1 genes encoding the two major tyrosine phosphatases, a low molecular weight family enzyme and a histidinol phosphate phosphoesterase family enzyme, respectively. Additionally, strains were tested in both in vitro and in vivo (mouse abscess) conditions. Both the Δltp1 and the Δphp1 mutants exhibit little transcriptional difference to the parental strain cultured in vitro, which would tend to exclude a significant role of the phosphatases in P. gingivalis gene regulation under nutrient-rich, low-stress conditions. While the Δphp1 mutant also clustered closely to the parental strain in the abscess condition, there were a number of differentially regulated genes (DEGs) associated with transporter systems. In the mouse abscess condition, DEGs in Δltp1 included one of the efflux ABC transporter systems also regulated in the Δphp1 mutant. However, the primary biological process populated by DGEs in Δltp1 involved genome stability. Comparison of the parental strain between the in vitro and in vivo condition indicated that DNA metabolic processes, including recombination and transposition, were significantly upregulated in vivo. Hence, Ltp1 specifically may be involved in the control of adaptation to in vivo conditions, while Ltp1 and Php1 have both common and enzyme-specific activities.

ORGANISM(S): Porphyromonas gingivalis

PROVIDER: GSE299059 | GEO | 2025/08/20

REPOSITORIES: GEO