Reconstitution of human ero1-l alpha/protein-disulfide isomerase oxidative folding pathway in vitro position-dependent differences in role between the a and a ' domains of protein-disulfide isomerase
文献类型：期刊论文
| 作者 | Wang, Lei1,2; Li, Sheng-jian1,2; Sidhu, Ateesh3; Zhu, Li1,2; Liang, Yi4; Freedman, Robert B.3; Wang, Chih-chen1 |
| 刊名 | Journal of biological chemistry
 |
| 出版日期 | 2009-01-02 |
| 卷号 | 284期号:1页码:199-206 |
| ISSN号 | 0021-9258 |
| DOI | 10.1074/jbc.m806645200 |
| 通讯作者 | Wang, chih-chen(chihwang@sun5.ibp.ac.cn) |
| 英文摘要 | Protein-disulfide isomerase (pdi), a critical enzyme responsible for oxidative protein folding in the eukaryotic endoplasmic reticulum, is composed of four thioredoxin domains a, b, b', a', and a linker x between b' and a'. ero1-l alpha, an oxidase for human pdi (hpdi), has been determined to have one molecular flavin adenine dinucleotide (fad) as its prosthetic group. oxygen consumption assays with purified recombinant ero1-l alpha revealed that it utilizes oxygen as a terminal electron acceptor producing one disulfide bond and one molecule of hydrogen peroxide per dioxygen molecule consumed. exogenous fad is not required for recombinant ero1-l alpha activity. by monitoring the reactivation of denatured and reduced rnase a, we reconstituted the ero1-l alpha/hpdi oxidative folding system in vitro and determined the enzymatic activities of hpdi in this system. mutagenesis studies suggested that the a' domain of hpdi is much more active than the a domain in ero1-l alpha-mediated oxidative folding. a domain swapping study revealed that one catalytic thioredoxin domain to the c-terminal of bb' x, whether a or a' , is essential in ero1-l alpha-mediated oxidative folding. these data, combined with a pull-down assay and isothermal titration calorimetry measurements, enabled the minimal element for binding with ero1-l alpha be mapped to the b' xa' fragment of hpdi. |
| WOS关键词 | ENDOPLASMIC-RETICULUM ; BOND FORMATION ; CRYSTAL-STRUCTURE ; BINDING SITE ; REDOX STATE ; GLUTATHIONE ; ERP57 ; YEAST ; ERO1 ; THIOREDOXIN |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| WOS记录号 | WOS:000261974800023 |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2401138 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Wang, Chih-chen |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England 4.Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Lei,Li, Sheng-jian,Sidhu, Ateesh,et al. Reconstitution of human ero1-l alpha/protein-disulfide isomerase oxidative folding pathway in vitro position-dependent differences in role between the a and a ' domains of protein-disulfide isomerase[J]. Journal of biological chemistry,2009,284(1):199-206. |
| APA | Wang, Lei.,Li, Sheng-jian.,Sidhu, Ateesh.,Zhu, Li.,Liang, Yi.,...&Wang, Chih-chen.(2009).Reconstitution of human ero1-l alpha/protein-disulfide isomerase oxidative folding pathway in vitro position-dependent differences in role between the a and a ' domains of protein-disulfide isomerase.Journal of biological chemistry,284(1),199-206. |
| MLA | Wang, Lei,et al."Reconstitution of human ero1-l alpha/protein-disulfide isomerase oxidative folding pathway in vitro position-dependent differences in role between the a and a ' domains of protein-disulfide isomerase".Journal of biological chemistry 284.1(2009):199-206. |
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来源：中国科学院大学
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