期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 2, 页码 1508-1515出版社
ELSEVIER
DOI: 10.1074/jbc.M109.053520
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资金
- Ministry of Education, Science and Culture of Japan
Atg16 interacts with the Atg12-Atg5 protein conjugate through its N-terminal domain and self-assembles through its coiled-coil domain (CCD). Formation of the Atg12-Atg5.Atg16 complex is essential for autophagy, the bulk degradation process conserved among most eukaryotes. Here, we report the crystal structures of full-length Saccharomyces cerevisiae Atg16 at 2.8 angstrom resolution and its CCD at 2.5 angstrom resolution. The CCD and full-length Atg16 each exhibit an extended alpha-helix, 90 and 130 angstrom, respectively, and form a parallel coiled-coil dimer in the crystals. Although the apparent molecular weight of Atg16 observed by gel-filtration chromatography suggests that Atg16 is tetrameric, an analytical ultracentrifugation study showed Atg16 as a dimer in solution, consistent with the crystal structure. Evolutionary conserved surface residues clustered at the C-terminal half of Atg16 CCD were shown to be crucial for autophagy. These results will give a structural basis for understanding the molecular functions and significance of Atg16 in autophagy.
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