The BECN1 N-terminal domain is intrinsically disordered
- Lee, EF; Perugini, MA; Pettikiriarachchi, A; Evangelista, M; Keizer, DW; Yao, S; Fairlie, WD;
Publication Year 2016-03-03, Volume 12, Issue #3, Page 460-71
- Journal Title
- Publication Type
- Journal Article
- BECN1/Beclin 1 has a critical role in the early stages of autophagosome formation. Recently, structures of its central and C-terminal domains were reported, however, little structural information is available on the N-terminal domain, comprising a third of the protein. This lack of structural information largely stems from the inability to produce this region in a purified form. Here, we describe the expression and purification of the N-terminal domain of BECN1 (residues 1 to 150) and detailed biophysical characterization, including NMR spectroscopy. Combined, our studies demonstrated at the atomic level that the BECN1 N-terminal domain is intrinsically disordered, and apart from the BH3 subdomain, remains disordered following interaction with a binding partner, BCL2L1/BCL-XL. In addition, the BH3 domain alpha-helix induced upon interaction with BCL2L1 reverts to a disordered state when the complex is dissociated by exposure to a competitive inhibitor. No significant interactions between N- and C-terminal domains were detected.
- Taylor & Francis
- WEHI Research Division(s)
- Structural Biology
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Creation Date: 2016-04-28 02:07:01Last Modified: 2016-05-02 09:48:07