Molecular Architecture of Yeast Chromatin Assembly Factor 1
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 26702Article in journal (Refereed) PublishedText
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.
Place, publisher, year, edition, pages
Nature Publishing Group, 2016. Vol. 6, 26702
IdentifiersURN: urn:nbn:se:kth:diva-188727DOI: 10.1038/srep26702ISI: 000376499900001PubMedID: 27221973ScopusID: 2-s2.0-84971317627OAI: oai:DiVA.org:kth-188727DiVA: diva2:939734
QC 201606202016-06-202016-06-172016-06-20Bibliographically approved