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. 2000 Sep 18;150(6):1507–1513. doi: 10.1083/jcb.150.6.1507

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Apg1–Apg13 association is required for autophagy, but not for the Cvt pathway. A, Apg1-binding site of Apg13. Interaction of the indicated Apg13 fragments (prey) with Apg1 (bait) in the yeast two-hybrid system. Binding activity was estimated by β-galactosidase activity (Kaiser et al. 1994, shown as means and errors calculated from three independent experiments). B, Apg1–Apg13 association is required specifically for autophagy. Wild-type cells (TN125) or apg13Δ cells (YYK130) harboring the indicated APG13 constructs grown in YEPD were analyzed by anti-API immunoblot (top). An ALP assay was performed after 4 h SD(−N) incubation (bottom). C, Apg1 kinase assay was performed using the above APG13 transformants before or after rapamycin (0.2 μg/ml, 1 h) treatment.

Apg1–Apg13 association is required for autophagy, but not for the Cvt pathway. A, Apg1-binding site of Apg13. Interaction of the indicated Apg13 fragments (prey) with Apg1 (bait) in the yeast two-hybrid system. Binding activity was estimated by β-galactosidase activity (Kaiser et al. 1994, shown as means and errors calculated from three independent experiments). B, Apg1–Apg13 association is required specifically for autophagy. Wild-type cells (TN125) or apg13Δ cells (YYK130) harboring the indicated APG13 constructs grown in YEPD were analyzed by anti-API immunoblot (top). An ALP assay was performed after 4 h SD(−N) incubation (bottom). C, Apg1 kinase assay was performed using the above APG13 transformants before or after rapamycin (0.2 μg/ml, 1 h) treatment.