Bacterial spore surface nanoenvironment requires a AAA plus ATPase to promote MurG function

• 成果类型: Article
• 署名作者: Delerue, Thomas; Updegrove, Taylor B.; Chareyre, Sylvia; Anantharaman, Vivek; Gilmore, Michael C.; Jenkins, Lisa M.; Popham, David L.; Cava, Felipe; Aravind, L.; Ramamurthi, Kumaran S.
• 署名单位: National Institutes of Health (NIH) - USA; NIH National Cancer Institute (NCI); National Institutes of Health (NIH) - USA; NIH National Library of Medicine (NLM); Division of Intramural Research (DIR); Umea University; National Institutes of Health (NIH) - USA; NIH National Cancer Institute (NCI); Virginia Polytechnic Institute & State University
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-11328
• DOI: 10.1073/pnas.2414737121
• 发表日期: 2024-10-22
• 关键词: bacillus-subtilis; morphogenetic protein; sporulation; coat; expression; DYNAMICS; mutants; spoiva; unit

摘要

Bacillus subtilis spores are produced inside the cytosol of a mother cell. Spore surface assembly requires the SpoVK protein in the mother cell, but its function is unknown. Here, we report that SpoVK is a sporulation- specific, forespore- localized putative chaperone from a distinct higher- order clade of AAA+ ATPases that promotes the peptidoglycan glycosyltransferase activity of MurG during sporulation, even though MurG does not normally require activation during vegetative growth. MurG redeploys to the forespore surface during sporulation, where we show that the local pH is reduced and propose that this change in cytosolic nanoenvironment abrogates MurG function. Further, we show that SpoVK participates in a developmental checkpoint in which improper spore surface assembly mis- localizes SpoVK, which leads to sporulation arrest. The AAA+ ATPase clade containing SpoVK includes specialized chaperones involved in secretion, cell envelope biosynthesis, and carbohydrate metabolism, suggesting that such fine- tuning might be a widespread feature of different subcellular nanoenvironments.