Dataset Information

Identification and characterization of the cell division protein MapZ from Streptococcus suis

ABSTRACT: Abstract Streptococcus suis, an emerging zoonotic pathogen, causes invasive diseases in pigs, including sepsis, meningitis, endocarditis, pneumonia, and arthritis. Importantly, similar pathologies are reported in human S. suis infections. In previous work, the locus SSU0375 of S. suis strain P1.7 had been identified as a conditionally essential gene by intrathecal experimental infection of pigs with a transposon library of S. suis. This study aimed to identify the function of the corresponding gene product. Bioinformatics analysis and homology modeling revealed sequence and structural homologies with the Streptococcus pneumoniae mid‐cell‐anchored protein Z (MapZ) that is involved in cell division in different bacterial species. Indeed, depletion of this locus in S. suis strain 10 revealed a growth defect as compared to the wild type. Electron microscopy analysis of the corresponding mutant demonstrated morphological growth defects as compared to the wild‐type strain, including an irregular cell shape and size as well as mispositioned division septa. Light microscopy and subsequent quantitative image analysis confirmed these morphological alterations. In the genetic rescue strain, the wild‐type phenotype was completely restored. In summary, we proposed that SSU0375 or the corresponding locus in strain 10 encode for a S. suis MapZ homolog that guides septum positioning as evidenced for other members of the Streptococci family. The mid‐cell anchored protein Z (MapZ) is involved in cell division in Streptococcus suis, an emerging zoonotic pathogen. The deletion of this gene leads to morphological growth defects including aberrant cell shapes and sizes as well as mispositioned division septa. Moreover, the absence of MapZ results in reduced biological fitness in the host.

SUBMITTER: Dresen M

PROVIDER: S-EPMC8501179 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Similar Datasets

Project description:FtsEX is a membrane complex widely conserved across diverse bacterial genera and involved in critical processes such as recruitment of division proteins and in spatial and temporal regulation of muralytic activity during cell division or sporulation. FtsEX is a member of the ABC transporter superfamily. The component FtsX is an integral membrane protein, whereas FtsE is an ATPase and is required for the transmission of a conformational signal from the cytosol through the membrane to regulate the activity of cell wall hydrolases in the periplasm. Both proteins are essential in the major human respiratory pathogenic bacterium Streptococcus pneumoniae, and FtsX interacts with the modular peptidoglycan hydrolase PcsB at the septum. Here, we report high-resolution structures of pneumococcal FtsE bound to different nucleotides. Structural analysis revealed that FtsE contains all the conserved structural motifs associated with ATPase activity and afforded interpretation of the in vivo dimeric arrangement in both the ADP and ATP states. Interestingly, three specific FtsE regions with high structural plasticity were identified that shape the cavity in which the cytosolic region of FtsX would be inserted. The residues corresponding to the FtsX coupling helix, responsible for contacting FtsE, were identified and validated by in vivo mutagenesis studies showing that this interaction is essential for cell growth and proper morphology.IMPORTANCE Bacterial cell division is a central process that requires exquisite orchestration of both the cell wall biosynthetic and lytic machineries. The essential membrane complex FtsEX, widely conserved across bacteria, plays a central role by recruiting proteins to the divisome apparatus and by regulating periplasmic muralytic activity from the cytosol. FtsEX is a member of the type VII family of the ABC-superfamily, but instead of being a transporter, it couples the ATP hydrolysis catalyzed by FtsE to mechanically transduce a conformational signal that provokes the activation of peptidoglycan (PG) hydrolases. So far, no structural information is available for FtsE. Here, we provide the structural characterization of FtsE, confirming its ATPase nature and revealing regions with high structural plasticity which are key for FtsE binding to FtsX. The complementary binding region in FtsX has also been identified and validated in vivo Our results provide evidence on how the difference between the ATP/ADP-bound states in FtsE would dramatically alter the interaction of FtsEX with the PG hydrolase PcsB in pneumococcal division.

Dataset Information

Identification and characterization of the cell division protein MapZ from Streptococcus suis

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets