title: 3' truncated tRNAArg is essential for in vitro specific cleavage of partially synthesized mouse 18S rRNA.
abstract: In vitro synthesized 5' portions of mouse 18S rRNA are cleaved efficiently at a specific site in partially purified extracts of mouse FM3A cells and several mouse tissues. This activity is composed of both protein and RNA, and can be reconstituted with the protein component in micrococcal nuclease-treated extracts and the RNA component in phenol-treated ones. The RNA component of about 65 nucleotides with the complementing activity was purified from total RNA in the partially purified FM3A cell extracts by polyacrylamide gel electrophoreses. Chemical sequencing of this RNA elucidated that it is tRNAArg lacking nine nucleotides from its 3' terminus. Ribonuclease H treatment directed by deoxyoligonucleotides complementary to tRNAArg completely abolishes the cleavage activity, supporting the above conclusion.
authors.affiliation: Department of Biochemistry, Hokkaido University School of Medicine, Sapporo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Nashimoto
mesh_terms: D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D004247:DNA; D004722:Endoribonucleases / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D012337:RNA, Ribosomal, 18S / Q000378:metabolism*; D012347:RNA, Transfer, Arg / Q000378:metabolism*; D015183:Restriction Mapping; D016914:Ribonuclease H / Q000378:metabolism
chemical_list: D012337:RNA, Ribosomal, 18S; D012347:RNA, Transfer, Arg; D004247:DNA; D004722:Endoribonucleases; D016914:Ribonuclease H; C070374:ribonuclease 65