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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

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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

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dc.contributor.author Xu, Huibin
dc.contributor.author Tai, Jeff
dc.contributor.author Ye, Hong
dc.contributor.author Kang, Cong Bao
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-09-13T06:26:25Z
dc.date.available 2012-09-13T06:26:25Z
dc.date.copyright 2006
dc.date.issued 2012-09-13
dc.identifier.citation 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.
dc.identifier.issn 0006-291X
dc.identifier.uri http://hdl.handle.net/10220/8517
dc.description.abstract 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.
dc.language.iso en
dc.relation.ispartofseries Biochemical and biophysical research communications
dc.rights © 2006 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochemical and Biophysical Research Communications, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.bbrc.2005.12.227].
dc.subject DRNTU::Science::Biological sciences.
dc.title The N-terminal domain of tumor suppressor p53 is involved in the molecular interaction with the anti-apoptotic protein Bcl-Xl
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1016/j.bbrc.2005.12.227
dc.description.version Accepted version

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