{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Sobala M"],"funding":["Narodowe Centrum Nauki","National Institutes of Health"],"pubmed_abstract":["In bacteria, the so-called stringent response is responsible for adaptation to changing environmental conditions. This response is mediated by guanosine derivatives [(p)ppGpp], synthesized by either large mono-functional RelA or bi-functional SpoT (synthesis and hydrolysis) enzymes in β<i>-</i> and γ<i>-</i>proteobacteria, such as <i>Escherichia coli</i>. In Firmicutes and α<i>-</i>, δ<i>-</i>, and \uD835\uDF00<i>-</i>proteobacteria, large bifunctional Rel-SpoT-homologs (RSH), often accompanied by small (p)ppGpp synthetases and/or hydrolases devoid of regulatory domains, are responsible for (p)ppGpp turnover. Here, we report on surprising <i>in vitro</i> and <i>in vivo</i> properties of an RSH enzyme from <i>Methylobacterium extorquens</i> (RSH<sub>Mex</sub>). We find that this enzyme possesses some"],"journal":["Frontiers in microbiology"],"pagination":["859"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6491832"],"repository":["biostudies-literature"],"pubmed_title":["<i>Methylobacterium extorquens</i> RSH Enzyme Synthesizes (p)ppGpp and pppApp <i>in vitro</i> and <i>in vivo</i>, and Leads to Discovery of pppApp Synthesis in <i>Escherichia coli</i>."],"pmcid":["PMC6491832"],"pubmed_authors":["Bruhn-Olszewska B","Sobala M","Cashel M","Potrykus K"],"additional_accession":[]},"is_claimable":false,"name":"<i>Methylobacterium extorquens</i> RSH Enzyme Synthesizes (p)ppGpp and pppApp <i>in vitro</i> and <i>in vivo</i>, and Leads to Discovery of pppApp Synthesis in <i>Escherichia coli</i>.","description":"In bacteria, the so-called stringent response is responsible for adaptation to changing environmental conditions. This response is mediated by guanosine derivatives [(p)ppGpp], synthesized by either large mono-functional RelA or bi-functional SpoT (synthesis and hydrolysis) enzymes in β<i>-</i> and γ<i>-</i>proteobacteria, such as <i>Escherichia coli</i>. In Firmicutes and α<i>-</i>, δ<i>-</i>, and \uD835\uDF00<i>-</i>proteobacteria, large bifunctional Rel-SpoT-homologs (RSH), often accompanied by small (p)ppGpp synthetases and/or hydrolases devoid of regulatory domains, are responsible for (p)ppGpp turnover. Here, we report on surprising <i>in vitro</i> and <i>in vivo</i> properties of an RSH enzyme from <i>Methylobacterium extorquens</i> (RSH<sub>Mex</sub>). We find that this enzyme possesses some","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2026-05-05T03:31:45.966Z","creation":"2025-05-29T20:25:32.229Z"},"accession":"S-EPMC6491832","cross_references":{"pubmed":["31068922"],"doi":["10.3389/fmicb.2019.00859"]}}