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Helmholtz Zentrum für Infektionsforschung Repository > Division of Molecular Biotechnology (MBIO) > Dept. Gene Regulation and Differentiation (RDIF) > Publikations of the AG Genomanalytik(GMAK) > Recruitment of the ATP-dependent chromatin remodeler dMi-2 to the transcribed region of active heat shock genes.


Please use this identifier to cite or link to this item: http://hdl.handle.net/10033/245183
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Title: Recruitment of the ATP-dependent chromatin remodeler dMi-2 to the transcribed region of active heat shock genes.
Authors: Mathieu, Eve-Lyne
Finkernagel, Florian
Murawska, Magdalena
Scharfe, Maren
Jarek, Michael
Brehm, Alexander
Affiliation: Institute for Molecular Biology and Tumor Research, Philipps-University, Emil-Mannkopff-Strasse 2, 35037 Marburg, Germany.
Citation: Recruitment of the ATP-dependent chromatin remodeler dMi-2 to the transcribed region of active heat shock genes. 2012, 40 (11):4879-91 Nucleic Acids Res.
Journal: Nucleic acids research
Issue Date: Jun-2012
URI: http://hdl.handle.net/10033/245183
DOI: 10.1093/nar/gks178
PubMed ID: 22362736
Abstract: The ATP-dependent chromatin remodeler dMi-2 can play both positive and negative roles in gene transcription. Recently, we have shown that dMi-2 is recruited to the hsp70 gene in a heat shock-dependent manner, and is required to achieve high transcript levels. Here, we use chromatin immunoprecipitation sequencing (ChIP-Seq) to identify other chromatin regions displaying increased dMi-2 binding upon heat shock and to characterize the distribution of dMi-2 over heat shock genes. We show that dMi-2 is recruited to the body of at least seven heat shock genes. Interestingly, dMi-2 binding extends several hundred base pairs beyond the polyadenylation site into the region where transcriptional termination occurs. We find that dMi-2 does not associate with the entire nucleosome-depleted hsp70 locus 87A. Rather, dMi-2 binding is restricted to transcribed regions. Our results suggest that dMi-2 distribution over active heat shock genes are determined by transcriptional activity.
Type: Article
Language: en
MeSH: Adenosine Triphosphatases
Animals
Autoantigens
Cells, Cultured
Drosophila Proteins
Drosophila melanogaster
Genetic Loci
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Heat-Shock Response
Transcription, Genetic
ISSN: 1362-4962
Appears in Collections: Publikations of the AG Genomanalytik(GMAK)

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