A two-component system affects the localization of a divisome protein in Streptococcus pneumoniae

CORTES PAULO R; JOSE ECHENIQUE; NICOLAS REINOSO; NUBIA YANDAR

Cordoba

Encuentro; LII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2016

SAIB

In bacteria, cell division is carried out by more than 15 proteins which assemble at midcell and constitute a complex named divisome.It has been described that signal transduction systems known as two-component systems (TCS), are involved in the coordination ofcell wall biosynthesis and cell division mechanism. To determine the putative contribution of pneumococcal TCS in the localization ofdivisome proteins, we performed a screening of 12 histidine kinase (hk) mutants of S. pneumoniae and we determined the localizationof FtsZ, FtsA, EzrA and StkP. For this purpose, we cloned and fused the ftsZ, ftsA, ezrA and stkP genes with the gfp gene in areplicative vector for S. pneumoniae. According to previous reports, the FtsZ-GFP, FtsA-GFP, EzrA-GFP and StkP-GFP fusionproteins showed normal localization in the wild-type strain. In particular, we analyzed an hk mutant, here referred as hk-cd mutant,which showed a typical localization patterns of divisome proteins as did in the wild-type strain, with the exception of the StkP-GFPprotein fusion. Approximately a 22% of the hk-cd cells showed an elongated morphology and an altered StkP-GFP localization withmultiple septum. These results suggested that this TCS is involved in the cell division mechanism and contribute to the localization ofStkP, one of the main coordinators of the cell division mechanism of S. pneumoniae.