{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361699995435012608.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1128/jb.01259-07"}},{"identifier":{"@type":"URI","@value":"https://journals.asm.org/doi/pdf/10.1128/JB.01259-07"}}],"dc:title":[{"@value":"Dissection of 16S rRNA Methyltransferase (KsgA) Function in\n            <i>Escherichia coli</i>"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            A 16S rRNA methyltransferase, KsgA, identified originally in\n            <jats:italic>Escherichia coli</jats:italic>\n            is highly conserved in all living cells, from bacteria to humans. KsgA orthologs in eukaryotes possess functions in addition to their rRNA methyltransferase activity.\n            <jats:italic>E. coli</jats:italic>\n            Era is an essential GTP-binding protein. We recently observed that KsgA functions as a multicopy suppressor for the cold-sensitive cell growth of an\n            <jats:italic>era</jats:italic>\n            mutant [Era(E200K)] strain (Q. Lu and M. Inouye, J. Bacteriol.\n            <jats:bold>180</jats:bold>\n            :5243-5246, 1998). Here we observed that although KsgA(E43A), KsgA(G47A), and KsgA(E66A) mutations located in the\n            <jats:italic>S</jats:italic>\n            -adenosylmethionine-binding motifs severely reduced its methyltransferase activity, these mutations retained the ability to suppress the growth defect of the Era(E200K) strain at a low temperature. On the other hand, a KsgA(R248A) mutation at the C-terminal domain that does not affect the methyltransferase activity failed to suppress the growth defect. Surprisingly,\n            <jats:italic>E. coli</jats:italic>\n            cells overexpressing wild-type KsgA, but not KsgA(R248A), were found to be highly sensitive to acetate even at neutral pH. Such growth inhibition also was observed in the presence of other weak organic acids, such as propionate and benzoate. These chemicals are known to be highly toxic at acidic pH by lowering the intracellular pH. We found that KsgA-induced cells had increased sensitivity to extreme acid conditions (pH 3.0) compared to that of noninduced cells. These results suggest that\n            <jats:italic>E. coli</jats:italic>\n            KsgA, in addition to its methyltransferase activity, has another unidentified function that plays a role in the suppression of the cold-sensitive phenotype of the Era(E200K) strain and that the additional function may be involved in the acid shock response. We discuss a possible mechanism of the KsgA-induced acid-sensitive phenotype.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699995435012609","@type":"Researcher","foaf:name":[{"@value":"Koichi Inoue"}],"jpcoar:affiliationName":[{"@value":"Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699995435012610","@type":"Researcher","foaf:name":[{"@value":"Soumit Basu"}],"jpcoar:affiliationName":[{"@value":"Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699995435012608","@type":"Researcher","foaf:name":[{"@value":"Masayori Inouye"}],"jpcoar:affiliationName":[{"@value":"Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219193"},{"@type":"EISSN","@value":"10985530"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/00219193"}],"prism:publicationName":[{"@value":"Journal of Bacteriology"}],"dc:publisher":[{"@value":"American Society for Microbiology"}],"prism:publicationDate":"2007-12","prism:volume":"189","prism:number":"23","prism:startingPage":"8510","prism:endingPage":"8518"},"reviewed":"false","dc:rights":["https://journals.asm.org/non-commercial-tdm-license"],"url":[{"@id":"https://journals.asm.org/doi/pdf/10.1128/JB.01259-07"}],"createdAt":"2007-09-22","modifiedAt":"2021-07-29","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050861770482354944","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004234621458176","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"GTPases involved in bacterial ribosome maturation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565165779113088","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"16S rRNA methyltransferase KsgA contributes to oxidative stress resistance and virulence in Staphylococcus aureus"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565167558385408","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"KsgA, a 16S rRNA adenine methyltransferase, has a novel DNA glycosylase/AP lyase activity to prevent mutations in Escherichia coli"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206409989248","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"ja","@value":"酸ストレスによる細菌細胞の損傷とその耐性機構"},{"@language":"en","@value":"Antibacterial Action of Acid Preservatives and Acid Stress Response in Bacteria"},{"@language":"ja-Kana","@value":"サン ストレス ニ ヨル サイキン サイボウ ノ ソンショウ ト ソノ タイセイ キコウ"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1128/jb.01259-07"},{"@type":"CROSSREF","@value":"10.1093/jb/mvt022_references_DOI_aKFDpd8uPjKrWVUp9QrnRNlyudM"},{"@type":"CROSSREF","@value":"10.3136/nskkk.65.148_references_DOI_aKFDpd8uPjKrWVUp9QrnRNlyudM"},{"@type":"CROSSREF","@value":"10.1016/j.biochi.2015.10.027_references_DOI_aKFDpd8uPjKrWVUp9QrnRNlyudM"},{"@type":"CROSSREF","@value":"10.1093/nar/gkp057_references_DOI_aKFDpd8uPjKrWVUp9QrnRNlyudM"},{"@type":"CROSSREF","@value":"10.1186/s41021-023-00266-5_references_DOI_aKFDpd8uPjKrWVUp9QrnRNlyudM"}]}