The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
Stepwise Histone Replacement by SWR1 Requires Dual Activation with Histone H2A.Z and Canonical Nucleosome
Open accessAbstract
Summary Histone variant H2A.Z-containing nucleosomes are incorporated at most eukaryotic promoters. This incorporation is mediated by the conserved SWR1 complex, which replaces histone H2A in canonical nucleosomes with H2A.Z in an ATP-dependent manner. Here, we show that promoter-proximal nucleosomes are highly heterogeneous for H2A.Z in Saccharomyces cerevisiae, with substantial representation of nucleosomes containing one, two, or no H2A.Z molecules. SWR1-catalyzed H2A.Z replacement in vitro occurs in a stepwise and unidirectional fashion, one H2A.Z-H2B dimer at a time, producing heterotypic nucleosomes as intermediates and homotypic H2A.Z nucleosomes as end products. The ATPase activity of SWR1 is specifically stimulated by H2A-containing nucleosomes without ensuing histone H2A eviction. Remarkably, further addition of free H2A.Z-H2B dimer leads to hyperstimulation of ATPase activity, eviction of nucleosomal H2A-H2B and deposition of H2A.Z-H2B. These results suggest that the combination of H2A-containing nucleosome and free H2A.Z-H2B dimer acting as both effector and substrate for SWR1 governs the specificity and outcome of the replacement reaction.
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Biogenesis and function of tRNA fragments during sperm maturation and fertilization in mammals
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Post-Translational Modifications of Histones That Influence Nucleosome Dynamics
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Martire, S., & Banaszynski, L. A. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0262-8 · Cited by 392
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Metadata
- Authors
- Luk, E., Ranjan, A., FitzGerald, P. C., Mizuguchi, G., Huang, Y., Wei, D., & Wu, C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 143
- Issue
- 5
- Pages
- 725-736
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2008675991
- Cited by
- 469
- References
- 56
- FWCI
- 7.09
- Type
- journal article
- Language
- en
- Open access
- bronze
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