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Conformational detection of p53's oligomeric state by FlAsH Fluorescence.

Abstract：

:The p53 tumor suppressor protein is a critical checkpoint in prevention of tumor formation, and the function of p53 is dependent on proper formation of the active tetramer. In vitro studies have shown that p53 binds DNA most efficiently as a tetramer, though inactive p53 is predicted to be monomeric in vivo. We demonstrate that FlAsH binding can be used to distinguish between oligomeric states of p53, providing a potential tool to explore p53 oligomerization in vivo. The FlAsH tetra-cysteine binding motif has been incorporated along the dimer and tetramer interfaces in the p53 tetramerization domain to create reporters for the dimeric and tetrameric states of p53, though the geometry of the four cysteines is critical for efficient FlAsH binding. Furthermore, we demonstrate that FlAsH binding can be used to monitor tetramer formation in real-time. These results demonstrate the potential for using FlAsH fluorescence to monitor protein-protein interactions in vivo.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Webber TM,Allen AC,Ma WK,Molloy RG,Kettelkamp CN,Dow CA,Gage MJ

doi

10.1016/j.bbrc.2009.04.073

subject

Has Abstract

pub_date

2009-06-19 00:00:00

pages

66-70

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00769-4

journal_volume

384

pub_type

杂志文章

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