{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mittermeier M"],"funding":["Deutsche Forschungsgemeinschaft","National Cancer Institute","NCI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS","NIH HHS"],"pagination":["871-885"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9018486"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(4)"],"pubmed_abstract":["Escherichia coli RfaH abrogates Rho-mediated polarity in lipopolysaccharide core biosynthesis operons, and ΔrfaH cells are hypersensitive to antibiotics, bile salts, and detergents. Selection for rfaH suppressors that restore growth on SDS identified a temperature-sensitive mutant in which 46 C-terminal residues of the RNA polymerase (RNAP) β' subunit are replaced with 23 residues carrying a net positive charge. Based on similarity to rpoC397, which confers a temperature-sensitive phenotype and resistance to bacteriophages, we named this mutant rpoC397*. We show that SDS resistance depends on a single nonpolar residue within the C397* tail, whereas basic residues are dispensable. In line with its mimicry of RfaH, C397* RNAP is resistant to Rho but responds to pause signals, NusA, and NusG "],"journal":["Molecular microbiology"],"pubmed_title":["A non-native C-terminal extension of the β' subunit compromises RNA polymerase and Rho functions."],"pmcid":["PMC9018486"],"funding_grant_id":["P30 CA016058","R01 GM067153","CA0168058","433623608","S10 OD018056","GM067153"],"pubmed_authors":["Gjorgjevikj D","Artsimovitch I","Wang B","Wahl MC","Mittermeier M","Said N"],"additional_accession":[]},"is_claimable":false,"name":"A non-native C-terminal extension of the β' subunit compromises RNA polymerase and Rho functions.","description":"Escherichia coli RfaH abrogates Rho-mediated polarity in lipopolysaccharide core biosynthesis operons, and ΔrfaH cells are hypersensitive to antibiotics, bile salts, and detergents. Selection for rfaH suppressors that restore growth on SDS identified a temperature-sensitive mutant in which 46 C-terminal residues of the RNA polymerase (RNAP) β' subunit are replaced with 23 residues carrying a net positive charge. Based on similarity to rpoC397, which confers a temperature-sensitive phenotype and resistance to bacteriophages, we named this mutant rpoC397*. We show that SDS resistance depends on a single nonpolar residue within the C397* tail, whereas basic residues are dispensable. In line with its mimicry of RfaH, C397* RNAP is resistant to Rho but responds to pause signals, NusA, and NusG ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-09T13:46:22.805Z","creation":"2025-02-18T23:45:04.246Z"},"accession":"S-EPMC9018486","cross_references":{"pubmed":["35049093"],"doi":["10.1111/mmi.14879"]}}