The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14
文献类型：期刊论文
| 作者 | Zhang, P; Zhao, JY; Wang, B; Du, JM; Lu, YC; Chen, JY; Ding, JP |
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2006 |
| 卷号 | 15期号:10页码:2423-2434 |
| 关键词 | chromatin remodeling MRG15 MRG domain PAM14 protein-protein interaction transcription regulation |
| 通讯作者 | Ding, JP (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,jpding@sibs.ac.cn |
| 英文摘要 | MRG15 is a transcription factor expressed in a variety of human tissues, and its orthologs have been found in many other eukaryotes which constitute the MRG protein family. It plays a vital role in embryonic development and cell proliferation, and is involved in cellular senescence. The C-terminal part of MRG15 forms a conserved MRG domain which is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein PAM14 during transcriptional regulation. We report here the characterization of the interaction between the MRG domain of human MRG15 and PAM14 using both yeast two-hybrid and in vitro binding assays based on the crystal structure of the MRG domain. The MRG domain is predominantly hydrophobic, and consists of mainly alpha-helices that are arranged in a three-layer sandwich topology. The hydrophobic core is stabilized by interactions among a number of conserved hydrophobic residues. The molecular surface is largely hydrophobic, but contains a few hydrophilic patches. Structure-based site-directed mutagenesis studies identified key residues involved in the binding of PAM14. Structural and biochemical data together demonstrate that the PAM14 binding site is consisted of residues Ile160, Leu168, Val169, Trp172, Tyr235, Val268, and Arg269 of MRG15, which form a shallow hydrophobic pocket to interact with the N-terminal 50 residues of PAM14 through primarily hydrophobic interactions. These results provide the molecular basis for the interaction between the MRG domain and PAM14, and reveal insights into the potential biological function of MRG15 in transcription regulation and chromatin remodeling. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | DOSAGE COMPENSATION COMPLEX ; MALE-SPECIFIC LETHAL-3 ; CHROMO-DOMAIN ; FUNCTIONAL-INTEGRATION ; RETINOBLASTOMA PROTEIN ; HISTONE DEACETYLASE ; CRYSTAL-STRUCTURE ; HP1 PROTEINS ; GENE ; IDENTIFICATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000240851300020 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1767]  |
| 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 | Zhang, P,Zhao, JY,Wang, B,et al. The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14[J]. PROTEIN SCIENCE,2006,15(10):2423-2434. |
| APA | Zhang, P.,Zhao, JY.,Wang, B.,Du, JM.,Lu, YC.,...&Ding, JP.(2006).The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14.PROTEIN SCIENCE,15(10),2423-2434. |
| MLA | Zhang, P,et al."The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14".PROTEIN SCIENCE 15.10(2006):2423-2434. |
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