北京大学医学部机构知识库
Advanced  
IR@PKUHSC  > 基础医学院  > 免疫学系  > 期刊论文
学科主题: 基础医学
题名:
Human TFDP3, a novel DP protein, inhibits DNA binding and transactivation by E2F
作者: Qiao, Huan; Di Stefano, Luisa; Tian, Chan; Li, Yun-Yan; Yin, Yan-Hui; Qian, Xiao-Ping; Pang, Xue-Wen; Li, Yan; McNutt, Michael Allen; Helin, Kristian; Zhang, Yu; Chen, Wei-Feng
刊名: JOURNAL OF BIOLOGICAL CHEMISTRY
发表日期: 2007-01-05
DOI: 10.1074/jbc.M606169200
卷: 282, 期:1, 页:454-466
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology
研究领域[WOS]: Biochemistry & Molecular Biology
关键词[WOS]: TRANSCRIPTION FACTOR DRTF1/E2F ; THYMIC NEGATIVE SELECTION ; CELL-CYCLE PROGRESSION ; FAMILY-MEMBER ; GROWTH SUPPRESSION ; APOPTOSIS ; PROLIFERATION ; EXPRESSION ; INDUCTION ; REPRESSOR
英文摘要:

The two known DP proteins, TFDP1 and -2, bind E2Fs to form heterodimers essential for high affinity DNA binding and efficient transcriptional activation/repression. Here we report the identification of a new member of the DP family, human TFDP3. Despite the high degree of sequence similarity, TFDP3 is apparently distinct from TFDP1 in function. Although TFDP3 retained the capacity to bind to E2F proteins, the resulting heterodimers failed to interact with the E2F consensus sequence. In contrast to the stimulatory effect of TFDP1, TFDP3 inhibited E2F-mediated transcriptional activation. Consistent with this observation, we found that ectopic expression of TFDP3 impaired cell cycle progression from G(1) to S phase instead of facilitating such a transition as TFDP1 does. Sequence substitution analysis indicated that the DNA binding domain of TFDP3 was primarily responsible for the lack of DNA binding ability of E2F-TFDP3 heterodimers and the inhibition of E2F-mediated transcriptional activation. Fine mapping further revealed four amino acids in this region, which were critical for the functional conversion from activation by TFDP1 to suppression by TFDP3. In conclusion, these studies identify a new DP protein and a novel mechanism whereby E2F function is regulated.

语种: 英语
WOS记录号: WOS:000243166500051
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/62581
Appears in Collections:基础医学院_免疫学系_期刊论文

Files in This Item:
File Name/ File Size Content Type Version Access License
J. Biol. Chem.-2007-Qiao-454-66.pdf(1125KB)期刊论文出版稿限制开放 联系获取全文

作者单位: 1.Peking Univ, Hlth Sci Ctr, Dept Immunol, Beijing 100083, Peoples R China
2.Peking Univ, Hlth Sci Ctr, Dept Pathol, Beijing 100083, Peoples R China
3.European Inst Oncol, Dept Expt Oncol, I-20141 Milan, Italy

Recommended Citation:
Qiao, Huan,Di Stefano, Luisa,Tian, Chan,et al. Human TFDP3, a novel DP protein, inhibits DNA binding and transactivation by E2F[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2007,282(1):454-466.
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Qiao, Huan]'s Articles
[Di Stefano, Luisa]'s Articles
[Tian, Chan]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Qiao, Huan]‘s Articles
[Di Stefano, Luisa]‘s Articles
[Tian, Chan]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
Add to CiteULike Add to Connotea Add to Del.icio.us Add to Digg Add to Reddit

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Copyright © 2007-2017  北京大学医学部 - Feedback
Powered by CSpace