A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome
文献类型：期刊论文
| 作者 | Xu, H; He, WJ; Liu, WY |
| 刊名 | ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
 |
| 出版日期 | 2004 |
| 卷号 | 427期号:1页码:30-40 |
| 关键词 | C4453-A4454 cleavage-site elongation factor Biota orientalis RNase rat 28S rRNA ribotoxin specific cleavage |
| 通讯作者 | Liu, WY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,wyliu@sibs.ac.cn |
| 英文摘要 | A unique ribonuclease named Biota orientalis ribonuclease (Biota orientalis RNase) is purified to homogeneity from mature seeds of oriental arborvitae (Biota orientalis). The molecular mass of Biota orientalis RNase is about 13 kDa. When the concentration of Mg(2+) is 25 mM in the incubation buffer, the ribonuclease specifically cleaves the phosphodiester bond between C4453 and A4454 in region K (a region in domain VII) of 28S RNA in rat ribosome, resulting in inactivation of ribosome. Thus, it is a ribotoxin similar to a-sarcin. The region around C4453-A4454 in rat 28S rRNA is named "Biota orientalis RNase region." Rat ribosome treated by Biota orientalis RNase produces a small RNA fragment (S-fragment) that contains 333 nucleotides from the 3'-terminus of rat 28S rRNA. The distance between the cleavage-sites of alpha-sarcin (G4325) and Biota orientalis RNase (C4453) is 128 nucleotides. Under restricted conditions (25 mM Mg(2+)), the substrate specificity of Biota orientalis RNase is extremely high: it acts only on the "Biota orientalis RNase region" of the largest RNA in ribosomes from certain eukaryotes. The ribosome specifically damaged by Biota orientalis RNase is unable to EF-1alpha-dependently bind aminoacyl-tRNA, whereas the formation of the EF-2/GDP/ribosome complex is not affected. It is proposed that Biota orientalis RNase inactivates ribosome at least partially by interfering with the EF-1alpha-dependent binding of aminoacyl-tRNA to ribosome. Biota orientalis RNase might be a useful tool in studying the structure/function of ribosome. (C) 2004 Elsevier Inc. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | SODIUM DODECYL-SULFATE ; POLYACRYLAMIDE-GEL ELECTROPHORESIS ; PROTEIN-SYNTHESIS ; EUKARYOTIC RIBOSOMES ; SARCIN/RICIN DOMAIN ; ENZYMATIC-ACTIVITY ; ELONGATION-FACTORS ; N-GLYCOSIDASE ; ALPHA-SARCIN ; IN-VITRO |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000222093200004 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2010]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Xu, H,He, WJ,Liu, WY. A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome[J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS,2004,427(1):30-40. |
| APA | Xu, H,He, WJ,&Liu, WY.(2004).A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome.ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS,427(1),30-40. |
| MLA | Xu, H,et al."A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome".ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 427.1(2004):30-40. |
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