AI Article Synopsis
- - Chromatin Assembly Complex 1 (CAF-1) is crucial for assembling histones H3 and H4 into nucleosomes, consisting of three subunits: p150, p60, and p48 in humans, and Cac1, Cac2, and Cac3 in yeast.
- - This study investigates the structure of yeast CAF-1 (yCAF-1) using advanced techniques like cross-linking mass spectrometry and electron microscopy to understand its molecular architecture.
- - Findings suggest that Cac1 is the largest subunit and likely acts as a key platform for binding histones, revealing that yCAF-1 has a bilobal shape and connects its subunits for effective histone chaperoning.
Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879628 | PMC |
| http://dx.doi.org/10.1038/srep26702 | DOI Listing |
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