Structure and function of the Orc1 BAH-nucleosome complex
Journal Article
·
· Nature Communications
- New York Univ. (NYU), NY (United States). School of Medicine; DOE/OSTI
- New York Univ. (NYU), NY (United States)
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States); New York University (NYU) Langone Health, NY (United States)
- New York Univ. (NYU), NY (United States). School of Medicine
- New York University (NYU) Langone Health, NY (United States)
The Origin Recognition Complex (ORC) is essential for replication, heterochromatin formation, telomere maintenance and genome stability in eukaryotes. Here we present the structure of the yeast Orc1 BAH domain bound to the nucleosome core particle. Our data reveal that Orc1, unlike its close homolog Sir3 involved in gene silencing, does not appear to discriminate between acetylated and non-acetylated lysine 16, modification states of the histone H4 tail that specify open and closed chromatin respectively. We elucidate the mechanism for this unique feature of Orc1 and hypothesize that its ability to interact with nucleosomes regardless of K16 modification state enables it to perform critical functions in both hetero- and euchromatin. We also show that direct interactions with nucleosomes are essential for Orc1 to maintain the integrity of rDNA borders during meiosis, a process distinct and independent from its known roles in silencing and replication.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- David and Lucile Packard Foundation; NYU School of Medicine; National Institutes of Health (NIH); USDOE
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1562715
- Journal Information:
- Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 10; ISSN 2041-1723
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
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