Open AccessBiophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
Author(s) -
Suzuki Hironori,
Noda Nobuo N.
Publication year - 2018
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12355
Subject(s) - autophagy , yeast , scaffold , scaffold protein , chemistry , characterization (materials science) , microbiology and biotechnology , biochemistry , biology , nanotechnology , computer science , materials science , signal transduction , apoptosis , database
Autophagy is an intracellular degradation system in which the formation of an autophagosome is a key event. In budding yeast, autophagosomes are generated from the preautophagosomal structure ( PAS ), in which Atg11 and Atg17 function as scaffolds essential for selective and nonselective types of autophagy, respectively. Structural studies have been extensively performed on Atg17, but not on Atg11, preventing us from understanding the selective type of the PAS . Here, we purified and characterized Atg11. Biophysical analyses, including analytical ultracentrifugation and CD, showed that Atg11 behaves as an elongated homodimer abundant in α‐helices in solution. Moreover, truncation analyses suggested that Atg11 has a parallel coiled‐coil architecture, in contrast to the antiparallel dimeric architecture of Atg17.