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

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 auto...

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Detalles Bibliográficos
Autores principales: Suzuki, Hironori, Noda, Nobuo N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5757174/
https://www.ncbi.nlm.nih.gov/pubmed/29321961
http://dx.doi.org/10.1002/2211-5463.12355
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author Suzuki, Hironori
Noda, Nobuo N.
author_facet Suzuki, Hironori
Noda, Nobuo N.
author_sort Suzuki, Hironori
collection PubMed
description 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.
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spelling pubmed-57571742018-01-10 Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast Suzuki, Hironori Noda, Nobuo N. FEBS Open Bio Research Articles 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. John Wiley and Sons Inc. 2017-12-04 /pmc/articles/PMC5757174/ /pubmed/29321961 http://dx.doi.org/10.1002/2211-5463.12355 Text en © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Suzuki, Hironori
Noda, Nobuo N.
Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title_full Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title_fullStr Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title_full_unstemmed Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title_short Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast
title_sort biophysical characterization of atg11, a scaffold protein essential for selective autophagy in yeast
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5757174/
https://www.ncbi.nlm.nih.gov/pubmed/29321961
http://dx.doi.org/10.1002/2211-5463.12355
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