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Cited by 304

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange

Open access
Smolle, Michaela, Venkatesh, Swaminathan, Gogol, Madelaine M, Li, Hua, Zhang, Ying, Florens, Laurence, Washburn, Michael P, Workman, Jerry L·2012·Nature Structural & Molecular Biology

Abstract

Set2-mediated methylation of histone H3 Lys36 (H3K36) is a mark associated with the coding sequences of actively transcribed genes, but it has a negative role during transcription elongation. It prevents trans-histone exchange over coding regions and signals for histone deacetylation in the wake of RNA polymerase II (RNAPII) passage. We have found that in Saccharomyces cerevisiae the Isw1b chromatin-remodeling complex is specifically recruited to open reading frames (ORFs) by H3K36 methylation through the PWWP domain of its Ioc4 subunit in vivo and in vitro. Isw1b acts in conjunction with Chd1 to regulate chromatin structure by preventing trans-histone exchange from taking place over coding regions. In this way, Isw1b and Chd1 are important in maintaining chromatin integrity during transcription elongation by RNAPII.

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Metadata

Authors
Smolle, M., Venkatesh, S., Gogol, M. M., Li, H., Zhang, Y., Florens, L., Washburn, M. P., & Workman, J. L.
Venue
Nature Structural & Molecular Biology
Published
2012-08-26
Volume
19
Issue
9
Pages
884-892
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2044946046
Cited by
304
References
4
FWCI
11.38
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange. https://app.cochat.ai/papers/10.1038/nsmb.2312
The paper
Smolle, M., Venkatesh, S., Gogol, M. M., Li, H., Zhang, Y., Florens, L., Washburn, M. P., & Workman, J. L. (2012). Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2312

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