Ionic conditions for the cleavage of the tRNA-like structure of turnip yellow mosaic virus by the catalytic RNA of RNase P
العنوان: | Ionic conditions for the cleavage of the tRNA-like structure of turnip yellow mosaic virus by the catalytic RNA of RNase P |
---|---|
المؤلفون: | Barbara S. Vold, R L Joshi, Christopher J. Green, M D Morch, A L Haenni |
المساهمون: | Joshi, Rajiv L., Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
المصدر: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1988, 263 (24), pp.11617-20 |
بيانات النشر: | HAL CCSD, 1988. |
سنة النشر: | 1988 |
مصطلحات موضوعية: | [SDV]Life Sciences [q-bio], viruses, MESH: Mosaic Viruses, MESH: Base Sequence, Biochemistry, MESH: Osmolar Concentration, RNA, Transfer, MESH: Magnesium, Magnesium, 0303 health sciences, Turnip yellow mosaic virus, biology, 030302 biochemistry & molecular biology, food and beverages, [SDV] Life Sciences [q-bio], MESH: Nucleic Acid Conformation, MESH: RNA, Viral, Transfer RNA, RNA, Viral, Electrophoresis, Polyacrylamide Gel, Bacillus subtilis, MESH: Endoribonucleases, RNase P, Molecular Sequence Data, Magnesium Chloride, Buffers, Cleavage (embryo), Ammonium Chloride, Ribonuclease P, 03 medical and health sciences, Mosaic Viruses, MESH: Ammonium Chloride, Endoribonucleases, MESH: RNA, Catalytic, RNA, Catalytic, Molecular Biology, 030304 developmental biology, MESH: Molecular Sequence Data, Mosaic virus, Base Sequence, Osmolar Concentration, fungi, RNA, MESH: Ribonuclease P, MESH: Magnesium Chloride, Cell Biology, MESH: Bacillus subtilis, biology.organism_classification, MESH: RNA, Transfer, A-site, Ionic strength, RNA, Ribosomal, MESH: RNA, Ribosomal, Nucleic Acid Conformation, MESH: Buffers, MESH: Electrophoresis, Polyacrylamide Gel |
الوصف: | International audience; The 3'-end of the RNA genome of turnip yellow mosaic virus can form a pseudoknotted tRNA-like structure that can be recognized by several tRNA-specific enzymes. We have found that the catalytic RNA component of Bacillus subtilis RNase P can cleave this structure in unusually low ionic strength buffers at a site analogous to the 5'-end of an aminoacyl stem of a tRNA. Most other precursors can only be processed under low ionic strength conditions if the RNase P holoenzyme is used; processing by the catalytic RNA component alone requires a higher ionic strength buffer. The cleavage of the turnip yellow mosaic virus tRNA-like structure demonstrates the importance of the substrate in determining the optimal buffer conditions for this reaction and also shows that high ionic strength buffers are not always necessary for cleavage by the catalytic RNA. |
اللغة: | English |
تدمد: | 0021-9258 1083-351X |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5a4a9f2e705adda5b2466de7541bf6f https://hal.archives-ouvertes.fr/hal-02160155 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....c5a4a9f2e705adda5b2466de7541bf6f |
قاعدة البيانات: | OpenAIRE |
تدمد: | 00219258 1083351X |
---|