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HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

ABSTRACT: We examined the RNA binding ability of the 70-kDa heat shock protein (HSP70) family member HSPA1A and HSP8 and identified the RNA species bound to HSP70 or HSP8 in vivo. We used a UV-crosslinkiung and immunoprecipitation based approach named FLASH-seq (Akta? et al., 2017) using 3xFLAG-Histidine-Biotin tagged ectopically expressed protein in HEK293T cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE191242 | GEO | 2024/01/17

REPOSITORIES: GEO

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HSP70 binds RNA and regulates transcription by RNA Polymerase III [RNA-seq]

Project description:We examined the RNA binding ability of the 70-kDa heat shock protein (HSP70) family member HSPA1A and identified the RNA species bound to HSP70 in vivo. We used a UV-crosslinkiung and immunoprecipitation based approach named FLASH-seq (Aktaş et al., 2017) using 3xFLAG-Histidine-Biotin tagged ectopically expressed protein in HEK293T cells.

2024-01-17 | GSE191244 | GEO

HSP70 binds RNA and regulates transcription by RNA Polymerase III [ChIP-seq]

2024-01-17 | GSE191243 | GEO

HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

Project description:HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

| PRJNA790738 | ENA

HSP70-driven molecular response to the proteasome machinery inhibition is a vulnerability in cancer

Project description:In this study we employed a label-free global proteomics approach, with a sensitivity of over 10k quantified proteins per sample, to determine contributions of different compensatory mechanisms upon the proteasome inhibition with carfilzomib - in cells of multiple myeloma, normal fibroblasts and cancers of lung, colon and pancreas. We identified several responding pathways, while the main HSP70 family stress inducible molecular chaperones HSPA1A and HSPA1B (often addressed jointly as HSPA1A/B or simply “Hsp70”, due to nearly identical protein sequences) were the most universal proteasome inhibition responders in proteomes of all the studied cell types. Further overlap of differential proteomics with RNA-seq analysis obtained at the same condions (DMSO control vs carfilzomib treatment) and a subsequent validation showed that the proteasome inhibition-dependent induction of HSPA1A/B and other chaperone proteins in cancer cells is in fact transcription-driven.

2022-09-22 | GSE184029 | GEO

Long Noncoding RNA RP11-115N4.1Promotes Inflammatory Responses by Interacting with HNRNPH3 and Enhancing the Transcription of HSP70 in Unexplained Recurrent Spontaneous Abortion

Project description:RP11-115N4.1 was identified as the most differentially expressed lncRNA which was highly upregulated in peripheral blood of non-pregnant URSA patients (P = 3.63E-07, Fold change = 2.96),andthis dysregulation was further validated in approximately 26.7% additional patients (4/15). RP11-115N4.1 expression was detected in both lymphocytes and monocytes of human peripheral blood, andin vitro overexpression of RP11-115N4.1 decreased cell proliferation in K562 cellssignificantly. Furthermore, heat-shock HSP70 genes (HSPA1A and HSPA1B) were found to be significantly upregulated upon RP11-115N4.1 overexpression by transcriptome analysis (HSPA1A (P = 4.39E-08, Fold change = 4.17), HSPA1B (P = 2.26E-06, Fold change = 2.99)).RNApull down and RNA immunoprecipitation assay (RIP) analysis demonstrated that RP11-115N4.1 bound to HNRNPH3 protein directly, which in turn activateheat-shock proteins (HSP70) analyzed by protein-protein interaction and HNRNP` knockdown assays. Most importantly,the high expression of HSP70 was also verified in the serum of URSA patients and the supernatant of K562 cells with RP11-115N4.1 activation, andHSP70 in supernatant can exacerbate inflammatory responses in monocytes by inducing IL-6, IL-1β and TNF-α and inhibit the migration of trophoblast cells, which might associate with URSA.

2021-08-11 | GSE179996 | GEO

MLF2-MBP purification (Table S4, Prophet et al.)

Project description:MLF2 was purified from mammalian Expi293 cells as a fusion with MBP. As MLF2 associates tightly with HSP70/HSPA1A, this resulted in a stoichiometric co-purification with HSP70 members. To identify which ones, we subjected the whole purification or a gel-extracted band around 70 kDa to mass spectrometry.

2022-08-23 | MSV000090188 | MassIVE

Hsp70 protects from stroke in atrial fibrillation patients by preventing thrombosis with no increased bleeding risk

Project description:Atrial fibrillation (AF) is a major risk factor for cardioembolic stroke. Anticoagulant drugs are effective in preventing AF-related stroke. However, the high frequency of anticoagulant-associated major bleeding is a major concern particularly when antiplatelet treatment is simultaneously administered. Here, microarray analysis in peripheral blood cells in eight patients with AF and stroke and eight AF subjects without stroke identified a stroke related gene expression pattern. HSPA1B, which encodes for heat-shock protein 70 kDa (Hsp70), was the most differentially expressed gene. This gene was downregulated in stroke subjects, a finding confirmed further in an independent AF cohort of 200 individuals. Hsp70 knock-out (KO) mice subjected to different thrombotic challenges developed thrombosis significantly earlier than their wild-type (WT) counterparts. In WT mice, Hsp70 inducers (TRC051384, or tubastatin A) delayed thrombus formation. Remarkably, Hsp70 inducers did not increase the bleeding risk even when aspirin was concomitantly administered. Hsp70 induction was associated with an increased vascular thrombomodulin expression, higher circulating levels of activated protein C (APC) upon thrombotic stimulus and increased protection against endothelial apoptosis. Thus, Hsp70 induction is a novel approach to delay thrombus formation with minimal bleeding risk, being especially promising in situations where there is a major bleeding hazard. Microarray analysis in peripheral blood cells includes eight patients with AF and stroke and eight AF subjects without stroke

2016-04-01 | E-GEOD-66724 | biostudies-arrayexpress

GNPS - MLF2-MBP purification (Table S4, Prophet et al.)

2022-08-23 | MSV000090188 | GNPS

Hsp70 protects from stroke in atrial fibrillation patients by preventing thrombosis with no increased bleeding risk

2016-04-01 | GSE66724 | GEO

Hsp70 and a Novel Axis of Type 1 Interferon-Dependent Antiviral Immunity in the Measles Virus-Infected Brain

Project description:The major inducible 70 kDa heat shock protein (hsp70) is host protective in a mouse model of measles virus (MeV) brain infection. Transgenic constitutive expression of hsp70 in neurons, the primary target of MeV infection, abrogates neurovirulence in neonatal H-2d congenic C57BL/6 mice. A significant level of protection is retained after depletion of T lymphocytes, implicating innate immune mechanisms. Focus of the present work was to elucidate the basis for hsp70-dependent innate immunity using this model. Transcriptome analysis of brains from transgenic (TG) and non-transgenic (NT) mice 5 days after infection identified type 1 interferon (IFN) signaling and macrophage activation/antigen presentation as the main differences linked to survival. The pivotal role for type 1 IFN in hsp70-mediated protection was demonstrated in mice with a genetically disrupted type 1 IFN receptor (IFNAR-/-), where IFNAR-/- eliminated the difference in survival between TG and NT mice. Brain macrophages, not neurons, are the predominant source of type 1 IFN in the virus-infected brain, and in vitro studies provided a mechanistic basis by which MeV-infected neurons can induce IFN-β in uninfected microglia in an hsp70-dependent manner. MeV infection induced extracellular release of hsp70 from mouse neuronal cells that constitutively express hsp70, and extracellular hsp70 induced IFN-β transcription in mouse microglial cells through Toll-like receptors 2 and 4. Collectively, results support a novel axis of type 1 IFN-dependent antiviral immunity in the virus-infected brain that is driven by hsp70.

2012-11-14 | GSE42264 | GEO

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