文献类型：期刊文献

英文题名：The Bacillus subtilis yqgC-sodA operon protects magnesium-dependent enzymes by supporting manganese efflux

作者：Sachla, Ankita J.[1];Soni, Vijay[2];Pineros, Miguel[3,4];Luo, Yuanchan[1,5];Im, Janice J.[1];Rhee, Kyu Y.[2];Helmann, John D.[1]

机构：[1]Cornell Univ, Dept Microbiol, Ithaca, NY 14850 USA;[2]Weill Cornell Med, Weill Dept Med, Div Infect Dis, New York, NY USA;[3]Cornell Univ, Sch Integrat Plant Sci, Plant Biol Sect, Ithaca, NY USA;[4]USDA ARS, Robert W Holley Ctr Agr & Hlth, Ithaca, NY USA;[5]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai, Peoples R China

年份：2024

卷号：206

期号：6

外文期刊名：JOURNAL OF BACTERIOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001236394000001)】；

基金：The authors acknowledge Shree Giri for conducting ICP-MS analyses, Eric Craft for the sample coordination, and Caitlin Leodis ('23) for technical assistance.

语种：英文

外文关键词：superoxide dismutase; manganese; magnesium; metal homeostasis

摘要：Microbes encounter a myriad of stresses during their life cycle. Dysregulation of metal ion homeostasis is increasingly recognized as a key factor in host-microbe interactions. Bacterial metal ion homeostasis is tightly regulated by dedicated metalloregulators that control uptake, sequestration, trafficking, and efflux. Here, we demonstrate that deletion of the Bacillus subtilis yqgC-sodA (YS) complex operon, but not deletion of the individual genes, causes hypersensitivity to manganese (Mn). YqgC is an integral membrane protein of unknown function, and SodA is a Mn-dependent superoxide dismutase (MnSOD). The YS strain has reduced expression of two Mn efflux proteins, MneP and MneS, consistent with the observed Mn sensitivity. The YS strain accumulated high levels of Mn, had increased reactive radical species (RRS), and had broad metabolic alterations that can be partially explained by the inhibition of Mg-dependent enzymes. Although the YS operon deletion strain and an efflux-deficient mneP mneS double mutant both accumulate Mn and have similar metabolic perturbations, they also display phenotypic differences. Several mutations that suppressed Mn intoxication of the mneP mneS efflux mutant did not benefit the YS mutant. Further, Mn intoxication in the YS mutant, but not the mneP mneS strain, was alleviated by expression of Mg-dependent, chorismate-utilizing enzymes of the menaquinone, siderophore, and tryptophan (MST) family. Therefore, despite their phenotypic similarities, the Mn sensitivity in the mneP mneS and the YS deletion mutants results from distinct enzymatic vulnerabilities.