Mechanism of
            <i>hsp70i</i>
            Gene Bookmarking

Xing, Hongyan; Wilkerson, Donald C.; Mayhew, Christopher N.; Lubert, Eric J.; Skaggs, Hollie S.; Goodson, Michael L.; Hong, Yan; Park-Sarge, Ok-Kyong; Sarge, Kevin D.

doi:10.1126/science.1106478

Cited by 159 publications

(196 citation statements)

References 20 publications

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“…HSF2 has previously been shown to bind to the hsp70i promoter during mitosis to mediate bookmarking of the hsp70i gene promoter [12]. Since our results showed that HSF2 and PRC1 interact during mitosis, we hypothesized that PRC1 could also be present at the hsp70i promoter.…”

Section: Prc1 Associates With the Hsp70i Promoter During Mitosismentioning

confidence: 63%

“…In this epigenetic mechanism, HSF2 bound to the hsp70i promoter recruits PP2A and inactivates the CAP-G subunit of condensin resulting in a region of DNA that remains "open" and allows for a rapid transition to a transcriptionally active state in early G1 of the cell cycle [12]. With the characterization of this phenomenon involving HSF2, the question remained as to whether other functions and interactions involving HSF2 in mitosis have yet to be discovered.…”

Section: Discussionmentioning

confidence: 99%

“…HeLa ATCC and Jurkat cells were treated with nocodazole (Sigma-Aldrich) at 250ng/mL for 18 hours or with 10nM Taxol (T7402 Sigma-Aldrich) for 24 hours [12,14,15]. For transfections, cells were transfected with pEGFP HSF2 or pEGFP-PRC1 using Effectene (Qiagen) or jetPEI (Bridge Bioscience) according to the manufacturer's instructions.…”

Section: Enrichment Of Mitotic Cell Populations/transient Transfectiomentioning

confidence: 99%

“…Jurkat cells were treated with nocodazole (250ng/mL for 18 hours) or Taxol (10nM for 24 hours) as indicated and subjected to ChIP analysis according to established protocols in our laboratory [12] with the following modifications. Pre-cleared chromatin was incubated with 13µg of goat PRC1 antibodies or control goat IgG, and rotated at 4°C for 16 hours.…”

Section: Chromatin Immunoprecipitation (Chip)mentioning

confidence: 99%

“…A study in our laboratory defined the mechanism by which heat shock transcription factor 2 (HSF2) mediates gene bookmarking at the hsp70i promoter, one of the promoters known to be bookmarked. Specifically, HSF2 binds to the heat shock elements (HSEs) in hsp70i and other heat shock gene promoters during mitosis and recruits the phosphatase PP2A, while simultaneously interacting with the CAP-G subunit of condensin to facilitate dephosphorylation/inactivation of adjacent condensin complexes, thereby reducing compaction of this specific region of chromosomal DNA in contrast to the majority of genomic DNA which remains compacted [12]. The reduced compaction at the hsp70i promoter allows rapid reassembly to a transcriptionally-competent state in early G1, which ensures the ability of the cell to induce this crucial proteoprotective heat shock protein if stress conditions occur [13].…”

Section: Introductionmentioning

confidence: 99%

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PRC1 associates with the hsp70i promoter and interacts with HSF2 during mitosis

Murphy

Wilkerson

Hong

et al. 2008

Experimental Cell Research

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Mitosis is a series of events leading to division of a cell by the process known as cytokinesis. Protein regulating cytokinesis 1 (PRC1) is a CDK substrate that associates with the mitotic spindle and functions in microtubule bundling. Previous studies revealed that loss of PRC1 is associated with chromosomal mis-segregation and atypical chromosome alignment. HSF2 is a DNA binding protein that we previously showed bookmarks the hsp70i gene during mitosis, an epigenetic mechanism which allows the hsp70i gene to re-establish transcriptional competence early in G1. Another study demonstrated that HSF2−/− mouse embryonic fibroblasts (MEFs) exhibit increased numbers of multinucleated cells vs. wild-type MEFs. This suggests that HSF2 is important for proper cytokinesis, but the mechanism was unknown. Here we report the existence of a direct interaction between HSF2 and PRC1. HSF2 and PRC1 associate during mitosis and co-localize during this phase of the cell cycle. PRC1 does not interact with the related protein HSF1, indicating the specificity of the HSF2-PRC1 interaction. Intriguingly, PRC1 is associated with the hsp70i promoter during mitosis. These results provide a potential mechanistic basis for the defective cytokinesis phenotype exhibited by HSF2−/− cells, as well as suggest a potential role for PRC1 in HSF2-mediated gene bookmarking.

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Section: Prc1 Associates With the Hsp70i Promoter During Mitosismentioning

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Section: Enrichment Of Mitotic Cell Populations/transient Transfectiomentioning

confidence: 99%

Section: Chromatin Immunoprecipitation (Chip)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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PRC1 associates with the hsp70i promoter and interacts with HSF2 during mitosis

Murphy

Wilkerson

Hong

et al. 2008

Experimental Cell Research

Self Cite

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JRK binds satellite III DNA and is necessary for the heat shock response

Waldron,

Rodriguez,

Williams

et al. 2024

Cell Biology International

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JRK is a DNA‐binding protein of the pogo superfamily of transposons, which includes the well‐known centromere binding protein B (CENP‐B). Jrk null mice exhibit epilepsy, and growth and reproductive disorders, consistent with its relatively high expression in the brain and reproductive tissues. Human JRK DNA variants and gene expression levels are implicated in cancers and neuropsychiatric disorders. JRK protein modulates β‐catenin–TCF activity but little is known of its cellular functions. Based on its homology to CENP‐B, we determined whether JRK binds centromeric or other satellite DNAs. We show that human JRK binds satellite III DNA, which is abundant at the chromosome 9q12 juxtacentromeric region and on Yq12, both sites of nuclear stress body assembly. Human JRK‐GFP overexpressed in HeLa cells strongly localises to 9q12. Using an anti‐JRK antiserum we show that endogenous JRK co‐localises with a subset of centromeres in non‐stressed cells, and with heat shock factor 1 following heat shock. Knockdown of JRK in HeLa cells proportionately reduces heat shock protein gene expression in heat‐shocked cells. A role for JRK in regulating the heat shock response is consistent with the mouse Jrk null phenotype and suggests that human JRK may act as a modifier of diseases with a cellular stress component.

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Heat shock transcription factor (Hsf)‐4b recruits Brg1 during the G1 phase of the cell cycle and regulates the expression of heat shock proteins

Tu¹,

Hu²,

Mivechi³

2006

J of Cellular Biochemistry

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Human brahma-related gene 1(Brg1) is a subunit of the switching/sucrose non-fermenting (SWI/SNF) chromatin-remodeling complex and regulates transcription during cell growth and differentiation and has been found to be mutated in many types of human cancers. Mammalian heat shock factor 1 (Hsf1), which binds conserved sequences on the promoter of the hsp70 gene when cells are exposed to various stress stimuli, utilizes Brg1-SWI/SNF complexes and stimulates transcription in vitro at the level of initiation and elongation. In contrast to the stress-inducibility of Hsf1, in vitro transcribed/translated Hsf4b binds to the heat shock element (HSE) constitutively and loses its ability to bind HSEs following stress. The regulation of Hsf4b transcriptional activity in vivo remains unclear. Here, we present evidence that Hsf4b recruits Brg1 complexes to the promoters of heat shock proteins (HSPs) under physiological growth conditions. Furthermore, in an asynchronous cell population, the association of Hsf4b with Brg1 complexes is regulated in response to activation/inactivation of the extracellular signal regulated protein kinase 1/2 (ERK1/2) signaling pathway. Since Brg1 is also the target of mitogen-activated protein (MAP) kinases and other protein kinases and it is hyperphosphorylated and inactivated during the G2/M phase of the cell cycle, we tested whether the association of Hsf4b with Brg1 complexes is altered during the cell cycle. The results indicate that association of Hsf4b with Brg1 complexes is undetectable during G2/M; however, an Hsf4b interaction with Brg1 complexes is evident at 1-3 h after progression of cells into G1, where chromatin structure is presumed to be more accessible to transcriptional regulatory proteins. At this time, Hsf4b exhibits increased DNA-binding activity and is detectable on promoters of multiple Hsps. To determine the unique role of Hsf4b in stimulating the expression of Hsps during the cell cycle, experiments were conducted with mouse embryo fibroblasts (MEFs) deficient in individual Hsfs. The results indicate that in the absence of Hsf1 and Hsf2, Hsf4b expression in cells leads to increased ability of Hsf4b to bind HSE during G1, leading to enhanced synthesis of inducible Hsp70.

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Mechanism of hsp70i Gene Bookmarking

Cited by 159 publications

References 20 publications

PRC1 associates with the hsp70i promoter and interacts with HSF2 during mitosis

PRC1 associates with the hsp70i promoter and interacts with HSF2 during mitosis

JRK binds satellite III DNA and is necessary for the heat shock response

Heat shock transcription factor (Hsf)‐4b recruits Brg1 during the G1 phase of the cell cycle and regulates the expression of heat shock proteins

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