Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast.

Abstract

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.