Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains
文献类型：期刊论文
| 作者 | Zhou, ZR; Zhang, YH; Liu, S; Song, AX; Hu, HY |
| 刊名 | BIOCHEMICAL JOURNAL
 |
| 出版日期 | 2012 |
| 卷号 | 441期号:1页码:143-149 |
| 关键词 | active-site crossover loop BRCA1 (breast cancer early-onset 1)-associated protein 1 (BAP1) ubiquitin C-terminal hydrolase (UCH) |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China.,hyhu@sibs.ac.cn |
| 英文摘要 | UCHs [Ub (ubiquitin) C-terminal hydrolases] are a family of deubiquitinating enzymes that are often thought to only remove small C-terminal peptide tails from Ub adducts. Among the four UCHs identified to date, neither UCH-L3 nor UCH-L1 can catalyse the hydrolysis of isopeptide Ub chains, but UCH-L5 can when it is present in the PA700 complex of the proteasome. In the present paper, we report that the UCH domain of UCH-L5, different from UCH-L1 and UCH-L3, by itself can process the K48-diUb (Lys(48)-linked di-ubiquitin) substrate by cleaving the isopeptide bond between two Ub units. The catalytic specificity of the four UCHs is dependent on the length of the active-site crossover loop. The UCH domain with a long crossover loop (usually >14 residues), such as that of UCH-L5 or BAPI [BRCA1 (breast cancer early-onset 1)-associated protein 1], is able to cleave both small and large Ub derivatives, whereas the one with a short loop can only process small Ub derivatives. We also found that elongation of the crossover loop enables UCH-L1 to have isopeptidase activity for K48-diUb in a length-dependent manner. Thus the loop length of UCHs defines their substrate specificity for diUb chains, suggesting that the chain flexibility of the crossover loop plays an important role in determining its catalytic activity and substrate specificity for cleaving isopeptide Ub chains. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | UCH37 DEUBIQUITINATING ENZYME ; BRCA1-ASSOCIATED PROTEIN-1 ; STRUCTURAL BASIS ; 26S PROTEASOME ; COMPLEX ; UCH-L1 ; IDENTIFICATION ; ISOPEPTIDASE ; ACTIVATION ; RESOLUTION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000298940900012 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/710]  |
| 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 | Zhou, ZR,Zhang, YH,Liu, S,et al. Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains[J]. BIOCHEMICAL JOURNAL,2012,441(1):143-149. |
| APA | Zhou, ZR,Zhang, YH,Liu, S,Song, AX,&Hu, HY.(2012).Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains.BIOCHEMICAL JOURNAL,441(1),143-149. |
| MLA | Zhou, ZR,et al."Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains".BIOCHEMICAL JOURNAL 441.1(2012):143-149. |
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