Structural and functional studies of cinnamomin, a new type II ribosome-inactivating protein isolated from the seeds of the camphor tree
文献类型：期刊论文
| 作者 | Xie, L; Wang, BZ; Hu, RG; Ji, HB; Zhang, L; Liu, WY |
| 刊名 | EUROPEAN JOURNAL OF BIOCHEMISTRY
 |
| 出版日期 | 2001 |
| 卷号 | 268期号:22页码:5723-5733 |
| 关键词 | cinnamomin expression mutagenesis ribosome-inactivating protein RNA N-glycosidase |
| 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 | Cinnamomin is a new type II ribosome-inactivating protein (RIP). Its A-chain exhibits RNA N-glycosidase activity to inactivate the ribosome and thus inhibit protein synthesis, whereas the glycosylated B-chain is a lectin. The primary structure of cinnamomin, which exhibits approximately 55% identity with those of ricin and abrin, was deduced from the nucleotide sequences of cDNAs of cinnamomin A- and B-chains. It is composed of a total of 549 amino-acid residues: 271 residues in the A-chain, a 14-residue linker and 264 residues in the B-chain. To explore its biological function, the cinnamomin A-chain was expressed in Escherichia coli with a yield of 100 mg per L of culture, and purified through two-step column chromatography. After renaturation, the recovery of the enzyme activity of the expressed A-chain was 80% of that of native A-chain. Based on the modeling of the three-dimensional structure of the A-chain, the functional roles of five amino acids and the only cysteine residues were investigated by site-directed mutagenesis or chemical modification. The conserved single mutation of the five amino-acid residues led to 8-50-fold losses of enzymatic activity, suggesting that these residues were crucial for maintaining the RNA N-glycosidase activity of the A-chain. Most interestingly, the strong electric charge introduced at the position of the single cysteine in A-chain seemed to play a role in enzyme/ substrate binding. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | RICIN-A-CHAIN ; POKEWEED ANTIVIRAL PROTEIN ; N-GLYCOSIDASE ACTIVITY ; B-CHAIN ; EUKARYOTIC RIBOSOMES ; ABRIN-A ; CRYSTAL-STRUCTURE ; DISULFIDE BOND ; AMINO-ACIDS ; RNA |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000172343000008 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2715]  |
| 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 | Xie, L,Wang, BZ,Hu, RG,et al. Structural and functional studies of cinnamomin, a new type II ribosome-inactivating protein isolated from the seeds of the camphor tree[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY,2001,268(22):5723-5733. |
| APA | Xie, L,Wang, BZ,Hu, RG,Ji, HB,Zhang, L,&Liu, WY.(2001).Structural and functional studies of cinnamomin, a new type II ribosome-inactivating protein isolated from the seeds of the camphor tree.EUROPEAN JOURNAL OF BIOCHEMISTRY,268(22),5723-5733. |
| MLA | Xie, L,et al."Structural and functional studies of cinnamomin, a new type II ribosome-inactivating protein isolated from the seeds of the camphor tree".EUROPEAN JOURNAL OF BIOCHEMISTRY 268.22(2001):5723-5733. |
入库方式： OAI收割
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。