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The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl

หน่วยงาน Nanyang Technological University, Singapore

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ชื่อเรื่อง : The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl
นักวิจัย : Xu, Huibin , Tai, Jeff , Ye, Hong , Kang, Cong Bao , Yoon, Ho Sup
คำค้น : DRNTU::Science::Biological sciences.
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2549
อ้างอิง : Xu, H., Tai, J., Ye, H., Kang, C. B., & Yoon, H. S. (2006). The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl. Biochemical and Biophysical Research Communications, 341(4), 938-944. , 0006-291X , http://hdl.handle.net/10220/8517 , http://dx.doi.org/10.1016/j.bbrc.2005.12.227
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Biochemical and biophysical research communications
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Emerging evidences suggest that transcription-independent mechanism of p53 appears to make an important contribution to the overall p53-dependent apoptosis. Recently, it has been postulated that the DNA-binding domain of p53 can interact with Bcl-Xl, and subsequently the proposed molecular interaction has been shown by NMR studies. Interestingly, Chipuk et al. [Cancer Cell 4 (2003) 371] reported that the N-terminal domain of p53 (p53NTD) alone is necessary and sufficient to induce transcription-independent apoptosis. To further define and understand the nature of the molecular recognition between p53 and Bcl-Xl, our current study focuses on p53NTD. We first demonstrated the molecular interaction between p53NTD and Bcl-Xl by co-expressing and purifying the complex. Second, to define the binding interface of the molecular interaction, which is not previously characterized, in the current we employed a NMR-based binding study, showing that the binding site on Bcl-Xl is located in the region including α4, the N- and C-termini of α3, the N-terminus of α5, and the central part of α2. To further probe this observation, we then performed fluorescence resonance energy transfer (FRET) assay in cells. The FRET efficiency detected between the donor and acceptor molecules appears to suggest the presence of molecular interaction of p53NTD with Bcl-Xl in cells. Taken together, our data suggest that p53NTD interacts with Bcl-Xl but the characteristic of the molecular interaction appears to be different from that of the DNA-binding domain of p53.

บรรณานุกรม :
Xu, Huibin , Tai, Jeff , Ye, Hong , Kang, Cong Bao , Yoon, Ho Sup . (2549). The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Xu, Huibin , Tai, Jeff , Ye, Hong , Kang, Cong Bao , Yoon, Ho Sup . 2549. "The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Xu, Huibin , Tai, Jeff , Ye, Hong , Kang, Cong Bao , Yoon, Ho Sup . "The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2549. Print.
Xu, Huibin , Tai, Jeff , Ye, Hong , Kang, Cong Bao , Yoon, Ho Sup . The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2549.