中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
In vitro interaction of eukaryotic elongation factor 2 with synthetic oligoribonucleotide that mimics GTPase domain of rat 28S ribosomal RNA

文献类型:期刊论文

作者He, WJ; Tang, SA; Liu, WY
刊名INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
出版日期2002
卷号34期号:3页码:263-268
关键词elongation factor 2 (eEF2) GTPase domain RNA GTP-binding protein ADP-ribosylation interaction
通讯作者Liu, WY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,
英文摘要Eukaryotic elongation factor 2 (eEF2) catalyzed the translocation of peptidyl-tRNA from the ribosomal A site to the P site. In this paper, the interaction between eEF2 and GTD RNA, a synthetic oligoribonucleotide that mimicked the GTPase domain of rat 28S ribosomal RNA, was Studied in vitro, The purified eEF2 could bind to GTD RNA, forming a stable complex. Transfer RNA competed with GTD RNA in binding to eEF2, whereas poly(A), poly(U) and poly(I,C) did not interfere with the interaction between eEF2 and GTD RNA, demonstrating that the tertiary structure of RNA might be necessary for the recognition of and binding to eEF2. The complex formation of eEF2 with GTD RNA was inhibited by SRD RNA, a synthetic oligoribonucleotide mimic of Sarcin/Ricin domain RNA of rat 28S RNA. Similarly, GTD RNA inhibited the interaction between eEF2 and SRD RNA. This fact implies that these small oligoribonucleotides probably share similar recognition or binding identity elements in their tertiary structures. In addition, the binding of eEF2 to GTD RNA could be obviously weakened by the ADP-ribosylation of eEF2 with diphtheria toxin. These results indicate that cEF2 behaves differently from prokaryotic EF-G in binding to ribosomal RNA. (C) 2002 Elsevier Science Ltd. All rights reserved.
学科主题Biochemistry & Molecular Biology; Cell Biology
类目[WOS]Biochemistry & Molecular Biology ; Cell Biology
关键词[WOS]FACTOR EF-G ; FACTOR-II ; ADP-RIBOSYLATION ; ANGSTROM-RESOLUTION ; PROTEIN-SYNTHESIS ; DIPHTHERIA-TOXIN ; BINDING ; POLYRIBOSOMES ; AUTOANTIBODY ; SUBUNIT
收录类别SCI
语种英语
WOS记录号WOS:000174113400006
版本出版稿
源URL[http://202.127.25.143/handle/331003/2471]  
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
He, WJ,Tang, SA,Liu, WY. In vitro interaction of eukaryotic elongation factor 2 with synthetic oligoribonucleotide that mimics GTPase domain of rat 28S ribosomal RNA[J]. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY,2002,34(3):263-268.
APA He, WJ,Tang, SA,&Liu, WY.(2002).In vitro interaction of eukaryotic elongation factor 2 with synthetic oligoribonucleotide that mimics GTPase domain of rat 28S ribosomal RNA.INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY,34(3),263-268.
MLA He, WJ,et al."In vitro interaction of eukaryotic elongation factor 2 with synthetic oligoribonucleotide that mimics GTPase domain of rat 28S ribosomal RNA".INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 34.3(2002):263-268.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。