The DOI matches its Crossref record.
Purification of a Human SRCAP Complex That Remodels Chromatin by Incorporating the Histone Variant H2A.Z into Nucleosomes
Abstract
The Snf-2-related CREB-binding protein activator protein (SRCAP) serves as a coactivator for a number of transcription factors known to interact with CBP. Swr1, the closest Saccharomyces cerevisiae ortholog of SRCAP, is a component of the chromatin remodeling complex SWR-C, which catalyzes exchange of the histone variant H2A.Z into nucleosomes. In this report, we use a combination of conventional chromatography and anti-SRCAP immunoaffinity chromatography to purify a native human SRCAP complex with a polypeptide composition similar to that of SWR-C, and we show for the first time that this SRCAP-containing complex supports ATP-dependent exchange of histone dimers containing H2B and H2A.Z into mononucleosomes reconstituted with recombinant H2A, H2B, H3, and H4. Our findings, together with previous evidence implicating H2A.Z in transcriptional regulation, suggest that SRCAP's coactivator function may depend on its ability to promote incorporation of H2A.Z into chromatin.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes
Clapier, C. R., Iwasa, J., Cairns, B. R., & Peterson, C. L. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.26 · Cited by 1,305
Chromatin remodelling during development
Ho, L., & Crabtree, G. R. (2010) · Nature · doi:10.1038/nature08911 · Cited by 1,114
ATP-dependent chromatin remodeling: genetics, genomics and mechanisms
Hargreaves, D. C., & Crabtree, G. R. (2011) · Cell Research · doi:10.1038/cr.2011.32 · Cited by 923
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Luk, E., Ranjan, A., FitzGerald, P. C., Mizuguchi, G., Huang, Y., Wei, D., & Wu, C. (2010) · Cell · doi:10.1016/j.cell.2010.10.019 · Cited by 469
The roles of histone variants in fine-tuning chromatin organization and function
Martire, S., & Banaszynski, L. A. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0262-8 · Cited by 392
Interaction of the Glucocorticoid Receptor with the Chromatin Landscape
John, S., Sabo, P. J., Johnson, T. A., Sung, M.-H., Biddie, S. C., Lightman, S. L., Voss, T. C., Davis, S. R., Meltzer, P. S., Stamatoyannopoulos, J. A., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.010 · Cited by 311
Chromatin remodelling beyond transcription: the INO80 and SWR1 complexes
Morrison, A. J., & Shen, X. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2693 · Cited by 311
ANP32E is a histone chaperone that removes H2A.Z from chromatin
Obri, A., Ouararhni, K., Papin, C., Diebold, M.-L., Padmanabhan, K., Marek, M., Stoll, I., Roy, L., Reilly, P. T., Mak, T. W., et al. (2014) · Nature · doi:10.1038/nature12922 · Cited by 272
p21 transcription is regulated by differential localization of histone H2A.Z
Gévry, N., Chan, H. M., Laflamme, L., Livingston, D. M., & Gaudreau, L. (2007) · Genes & Development · doi:10.1101/gad.1545707 · Cited by 266
Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics
Sardiu, M. E., Cai, Y., Jin, J., Swanson, S. K., Conaway, R. C., Conaway, J. W., Florens, L., & Washburn, M. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706983105 · Cited by 226
Self-citationMossink, B., Negwer, M., Schubert, D., & Nadif Kasri, N. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03714-5 · Cited by 114
H2A.Z: a molecular rheostat for transcriptional control
Subramanian, V., Fields, P. A., & Boyer, L. A. (2015) · F1000Prime Reports · doi:10.12703/p7-01 · Cited by 102
Hainer, S. J., & Fazzio, T. G. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.08.071 · Cited by 33
Metadata
- Authors
- Ruhl, D. D., Jin, J., Cai, Y., Swanson, S., Florens, L., Washburn, M. P., Conaway, R. C., Conaway, J. W., & Chrivia, J. C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-04-07
- Volume
- 45
- Issue
- 17
- Pages
- 5671-5677
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2088641994
- Cited by
- 266
- References
- 0
- FWCI
- 5.28
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.