title: Specific inhibition of bacterial RNase T2 by helix 41 of 16S ribosomal RNA.
abstract: Ribonuclease (RNase) T2 is involved in scavenging exogenous RNAs in the periplasmic                 space of bacteria. In Escherichia coli, although the 30S ribosomal subunit                 has long been known as a specific inhibitor of RNase T2 (designated as RNase I in                     E. coli), both the biochemical mechanisms and physiological roles of this                 interaction remain to be elucidated. Here we show, by creating hybrid ribosomes and                 mutational studies, that helix 41 (h41) of the E. coli 16S ribosomal RNA has                 a crucial role in the specific inhibition of RNase I. Notably, h41-mutant strains                 exhibit a lower survival rate at stationary phase and severe cell lysis when the                 post-segregation killing protein SrnB is expressed. These phenotypic defects                 accompany significant RNA degradation caused by RNase I. Thus, h41 in 16S rRNA                 provides a physiological benefit for the host cells in coping with the potential                 cytotoxicity of RNase T2.
authors: Bioproduction Research Institute, National Institute of Advanced                     Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-higashi,                 Toyohira-ku, Sapporo, Hokkaido                 062-8517, Japan.
authors: Kei
authors: K
authors: Kitahara
authors: Kentaro
authors: K
authors: Miyazaki
mesh_terms: D004722:Endoribonucleases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D009690:Nucleic Acid Conformation; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000235:genetics*; D049920:Ralstonia pickettii; D012705:Serratia
chemical_list: D012336:RNA, Ribosomal, 16S; D004722:Endoribonucleases; C022543:ribonuclease T(2)