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Endospore-forming bacteria also assemble a highly conserved essential membrane complex, called the A-Q complex, that physically connects these cells and may serve as a molecular conduit between them. While SpoIIIL was previously identified as a putative A-Q complex component in\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    , its exact role remains unclear. Here, we found that SpoIIIL does not function in the A-Q complex but instead acts as a forespore-specific factor required for efficient cell-cell signalling that leads to late mother cell transcription. Quantitative image analysis revealed that\n                    <jats:italic>spoIIIL<\/jats:italic>\n                    mutant spores do not exhibit hallmark phenotypes of A-Q complex mutants. Furthermore, unlike well-characterized A-Q complex proteins, SpoIIIL-GFP localizes uniformly in the forespore membrane before dispersing into the forespore cytoplasm. A synthetic sporulation screen identified a genetic relationship between\n                    <jats:italic>spoIIIL<\/jats:italic>\n                    and\n                    <jats:italic>murAB<\/jats:italic>\n                    , a paralog of\n                    <jats:italic>murAA<\/jats:italic>\n                    , required for efficient peptidoglycan precursor synthesis during sporulation. Cytological analysis indicates that the\n                    <jats:italic>spoIIIL murAB<\/jats:italic>\n                    double mutant is severely defective in the assembly of spore cortex peptidoglycan. Investigations into how SpoIIIL affects the cortex suggest it contributes to the activity of SpoIVB, a secreted forespore protease that initiates the signalling pathway required for processing of inactive pro-\u03c3K to active \u03c3K in the mother cell, which in turn up-regulates peptidoglycan precursor synthesis required for cortex formation. Accordingly, the\n                    <jats:italic>spoIIIL<\/jats:italic>\n                    mutant exhibits delayed and reduced pro-\u03c3K processing and decreased accumulation of peptidoglycan precursors. Thus, cortex assembly defects in the\n                    <jats:italic>spoIIIL murAB<\/jats:italic>\n                    double mutant results from alterations in separate pathways contributing to peptidoglycan precursor synthesis. Finally, phylogenetic analyses reveal that SpoIIIL is restricted to a subset of\n                    <jats:italic>Bacillales<\/jats:italic>\n                    species, highlighting evolutionary specialization in the signalling pathway leading to \u03c3K activation. Collectively, our findings redefine SpoIIIL as a forespore factor required for efficient cell-cell signalling that controls late mother-cell transcription.\n                  <\/jats:p>","DOI":"10.1371\/journal.pgen.1011768","type":"journal-article","created":{"date-parts":[[2025,7,3]],"date-time":"2025-07-03T16:02:54Z","timestamp":1751558574000},"page":"e1011768","update-policy":"https:\/\/doi.org\/10.1371\/journal.pgen.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["SpoIIIL is a forespore factor required for efficient cell-cell signalling during Bacillus subtilis sporulation"],"prefix":"10.1371","volume":"21","author":[{"given":"Danae","family":"Morales Angeles","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-4505-9652","authenticated-orcid":true,"given":"Kaitlyn","family":"Coleman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-3390-4833","authenticated-orcid":true,"given":"Chimezie","family":"Progress Odika","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4271-6731","authenticated-orcid":true,"given":"Chris","family":"L. 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