AUTHOR=Li Miaomaio , Gašparovič Henrich , Weng Xing , Chen Si , Korduláková Jana , Jessen-Trefzer Claudia 

TITLE=The Two-Component Locus MSMEG_0244/0246 Together With MSMEG_0243 Affects Biofilm Assembly in M. smegmatis Correlating With Changes in Phosphatidylinositol Mannosides Acylation

JOURNAL=Frontiers in Microbiology

VOLUME=11

YEAR=2020

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2020.570606

DOI=10.3389/fmicb.2020.570606

ISSN=1664-302X

ABSTRACT=<p>Ferric and ferrous iron is an essential transition metal for growth of many bacterial species including mycobacteria. The genomic region <italic>msmeg_0234</italic> to <italic>msmeg_0252</italic> from <italic>Mycobacterium smegmatis</italic> is putatively involved in iron/heme metabolism. We investigate the genes encoding the presumed two component system MSMEG_0244/MSMEG_0246, the neighboring gene <italic>msmeg_0243</italic> and their involvement in this process. We show that purified MSMEG_0243 indeed is a heme binding protein. Deletion of <italic>msmeg_0243</italic>/<italic>msmeg_0244/msmeg_0246</italic> in <italic>Mycobacterium smegmatis</italic> leads to a defect in biofilm formation and colony growth on solid agar, however, this phenotype is independent of the supplied iron source. Further, analysis of the corresponding mutant and its lipids reveals that changes in morphology and biofilm formation correlate with altered acylation patterns of phosphatidylinositol mannosides (PIMs). We provide the first evidence that <italic>msmeg_0244/msmeg_0246</italic> work in concert in cellular lipid homeostasis, especially in the maintenance of PIMs, with the heme-binding protein MSMEG_0243 as potential partner.</p>