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Title: The BECN1 N-terminal domain is intrinsically disordered.
Austin Authors: Lee, Erinna F;Perugini, Matthew A;Pettikiriarachchi, Anne;Evangelista, Marco;Keizer, David W;Yao, Shenggen;Fairlie, W Douglas
Affiliation: The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia
Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia
Olivia Newton-John Cancer Research Institute, Heidelberg, Victoria, Australia
School of Cancer Medicine, La Trobe University, Melbourne, Victoria, Australia
Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia
Department of Chemistry and Physics, La Trobe Institute for Molecular Science, Melbourne, Victoria, Australia
Issue Date: 2016
Publication information: Autophagy 2016; 12(3): 460-471
Abstract: 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 α-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.
DOI: 10.1080/15548627.2016.1140292
Journal: Autophagy
PubMed URL: 27046249
Type: Journal Article
Subjects: BCL2
BH3 domain
Beclin 1
intrinsically disordered protein; nuclear magnetic resonance
Appears in Collections:Journal articles

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