The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Transcriptional activation triggers deposition and removal of the histone variant H3.3
Open accessAbstract
DNA in eukaryotic cells is packaged into nucleosomes, the structural unit of chromatin. Both DNA and bulk histones are extremely long-lived, because old DNA strands and histones are retained when chromatin duplicates. In contrast, we find that the Drosophila HSP70 genes rapidly lose histone H3 and acquire variant H3.3 histones as they are induced. Histone replacement does not occur at artificial HSP70 promoter arrays, demonstrating that transcription is required for H3.3 deposition. The H3.3 histone is enriched in all active chromatin and throughout large transcription units, implying that deposition occurs during transcription elongation. Strikingly, we observed that the stability of chromatin-bound H3.3 differs between loci: H3.3 turns over at continually active rDNA genes, but becomes stable at induced HSP70 genes that have shut down. We conclude that H3.3 deposition is coupled to transcription, and continues while a gene is active. Repeated histone replacement suggests a mechanism to both maintain the structure of chromatin and access to DNA at active genes.
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From Silencing to Gene Expression
Janicki, S. M., Tsukamoto, T., Salghetti, S. E., Tansey, W. P., Sachidanandam, R., Prasanth, K. V., Ried, T., Shav-Tal, Y., Bertrand, E., Singer, R. H., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00171-0 · Cited by 704
Kinetics of Core Histones in Living Human Cells
Kimura, H., & Cook, P. R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1341 · Cited by 675
Adkins, M. W., Howar, S. R., & Tyler, J. K. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.016 · Cited by 294
Cited by
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Identification of long-lived proteins reveals exceptional stability of essential cellular structures
Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., & Hetzer, M. W. (2013) · Cell · doi:10.1016/j.cell.2013.07.037 · Cited by 572
Molecular dissection of formation of senescence-associated heterochromatin foci
Zhang, R., Chen, W., & Adams, P. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02019-06 · Cited by 415
Heterochromatin formation in the mouse embryo requires critical residues of the histone variant H3.3
Santenard, A., Ziegler-Birling, C., Koch, M., Tora, L., Bannister, A. J., & Torres-Padilla, M.-E. (2010) · Nature Cell Biology · doi:10.1038/ncb2089 · Cited by 300
Local and global influences on protein turnover in neurons and glia
Dörrbaum, A. R., Kochen, L., Langer, J. D., & Schuman, E. M. (2018) · eLife · doi:10.7554/elife.34202 · Cited by 249
Metadata
- Authors
- Schwartz, B. E., & Ahmad, K.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2005-03-17
- Volume
- 19
- Issue
- 7
- Pages
- 804-814
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2113451554
- Cited by
- 319
- References
- 4
- Type
- posted content
- Language
- en
- Open access
- diamond
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