Structural characterization of the sporulation protein GerM from Bacillus subtilis

• Published in: Journal of structural biology 2018-12, Vol.204 (3), p.481-490
• Main Authors: Trouve, Jennyfer, Mohamed, Ahmed, Leisico, Francisco, Contreras-Martel, Carlos, Liu, Bowen, Mas, Caroline, Rudner, David Z., Rodrigues, Christopher D.A., Morlot, Cecile
• Format: Article
• Language: English
• Subjects: Bacteriology; Endospores; GerM; GerMN domain; Life Sciences; Microbiology and Parasitology; SigG; Specialized secretion systems; Sporulation
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2018.09.010

[Display omitted] •The sporulation protein GerM contains 2 GerMN domains arranged in a butterfly shape.•GerMN domains can display different conformations.•GerMN domains display structural similarities with ring-building motifs. The Gram-positive bacterium Bacillus subtilis responds to starvation by entering a morphological differentiation process leading to the formation of a highly resistant spore. Early in the sporulation process, the cell asymmetrically divides into a large compartment (the mother cell) and a smaller one (the forespore), which will maturate into a resistant spore. Proper development of the forespore requires the assembly of a multiprotein complex called the SpoIIIA-SpoIIQ complex or “A-Q complex”. This complex involves the forespore protein SpoIIQ and eight mother cell proteins (SpoIIIAA to SpoIIIAH), many of which share structural similarities with components of specialized secretion systems and flagella found in Gram-negative bacteria. The assembly of the A-Q complex across the two membranes that separate the mother cell and forespore was recently shown to require GerM. GerM is a lipoprotein composed of two GerMN domains, a family of domains with unknown function. Here, we report X-ray crystallographic structures of the first GerMN domain of GerM at 1.0 Å resolution, and of the soluble domain of GerM (the tandem of GerMN domains) at 2.1 Å resolution. These structures reveal that GerMN domains can adopt distinct conformations and that the core of these domains display structural similarities with ring-building motifs found in components of specialized secretion system and in SpoIIIA proteins. This work provides an additional piece towards the structural characterization of the A-Q complex.