Journal
CELL STRESS & CHAPERONES
Volume 12, Issue 3, Pages 283-290Publisher
ALLIANCE COMMUNICATIONS GROUP DIVISION ALLEN PRESS
DOI: 10.1379/CSC-250.1
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Funding
- NICHD NIH HHS [F32 HD050043, F32HD050043] Funding Source: Medline
- NIEHS NIH HHS [ES007266, T32 ES007266] Funding Source: Medline
- NIGMS NIH HHS [R01 GM064606, R01 GM061053] Funding Source: Medline
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Although the vast majority of genomic DNA is tightly compacted during mitosis, the promoter regions of a number of genes remain in a less compacted state throughout this stage of the cell cycle. The decreased compaction of these promoter regions, which is referred to as gene bookmarking, is thought to be important for the ability of cells to express these genes during the following interphase. Previously, we reported a role for the DNA-binding protein heat shock factor (HSF2) in bookmarking the stress-inducible 70 000-Da heat shock protein (hsp70) gene. In this report, we have extended those studies and found that during mitosis, HSF2 is bound to the HSE promoter elements of other heat shock genes, including hsp90 and hsp27, as well as the proto-oncogene c-fos. The presence of HSF2 is important for expression of these genes because blocking HSF2 levels by RNA interference techniques leads to decreased levels of these proteins. These results suggest that HSF2 is important for constitutive as well as stress-inducible expression of HSE-containing genes.
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