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   <subfield code="a">10.3929/ethz-b-000117252</subfield>
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   <subfield code="a">10.1038/srep26702</subfield>
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   <subfield code="a">Molecular Architecture of Yeast Chromatin Assembly Factor 1</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Daegeun Kim, Dheva Setiaputra, Taeyang Jung, Jaehee Chung, Alexander Leitner, Jungmin Yoon, Ruedi Aebersold, Hans Hebert, Calvin K. Yip, Ji-Joon Song]</subfield>
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   <subfield code="a">Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes.</subfield>
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