title: RNase III mediated cleavage of the coding region of mraZ mRNA is required for efficient cell division in Corynebacterium glutamicum.
abstract: The Corynebacterium glutamicum R cgR_1959 gene encodes an endoribonuclease of the RNase III family. Deletion mutant of cgR_1959 (Δrnc mutant) showed an elongated cell shape, and presence of several lines on the cell surface, indicating a required of RNase III for maintaining normal cell morphology in C. glutamicum. The level of mraZ mRNA was increased, whereas cgR_1596 mRNA encoding a putative cell wall hydrolase and ftsEX mRNA were decreased in the Δrnc mutant. The half-life of mraZ mRNA was significantly prolonged in the Δrnc and the Δpnp mutant strains. This indicated that the degradation of mraZ mRNA was performed by RNase III and the 3'-to-5' exoribonuclease, PNPase. Northern hybridization and primer extension analysis revealed that the cleavage site for mraZ mRNA by RNase III is in the coding region. Overproduction of MraZ resulted in an elongated cell shape. The expression of ftsEX decreased while that of cgR_1596 unchanged in an MraZ-overexpressing strain. An electrophoretic mobility shift assay and a transcriptional reporter assay indicate that MraZ is a transcriptional repressor of ftsEX in C. glutamicum. These results indicate that RNase III is required for efficient expression of MraZ-dependent ftsEX and MraZ-independent cgR_1596.
authors.affiliation: Research Institute of Innovative Technology for the Earth, Kyoto, Japan.
authors.forename: Tomoya
authors.initials: T
authors.lastname: Maeda
authors.affiliation: Research Institute of Innovative Technology for the Earth, Kyoto, Japan.
authors.forename: Yuya
authors.initials: Y
authors.lastname: Tanaka
authors.affiliation: Research Institute of Innovative Technology for the Earth, Kyoto, Japan.
authors.forename: Norihiko
authors.initials: N
authors.lastname: Takemoto
authors.affiliation: Research Institute of Innovative Technology for the Earth, Kyoto, Japan.|Graduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
authors.forename: Nagisa
authors.initials: N
authors.lastname: Hamamoto
authors.affiliation: Research Institute of Innovative Technology for the Earth, Kyoto, Japan.|Graduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
authors.forename: Masayuki
authors.initials: M
authors.lastname: Inui
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D002455:Cell Division / Q000502:physiology; D048230:Corynebacterium glutamicum / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D016366:Open Reading Frames; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D043244:Ribonuclease III / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D012333:RNA, Messenger; D014157:Transcription Factors; D043244:Ribonuclease III