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. 2019 Feb 22;9:2592. doi: 10.1038/s41598-019-39292-1

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Arc/Arg3.1 reduces HSF1 affinity to HSE and interferes with cellular chaperone activity. (a) HEK293T cells were exposed to heat shock at 45°C for 15 min and crosslinked with formaldehyde. Chromatin immunoprecipitation using rabbit IgG or anti-HSF1 antibody was performed. Immunoprecipitated HSE region of hsp70 was quantified using quantitative real-time PCR. (b) HEK293T cells were transfected with HA-HSF1 and hsp27-luciferase plasmed with empty vector or Flag-Arc vector. After 24 h, luciferase activity was measured. (c) HEK293T cells were transfected with Flag empty vector or Flag-Arc and heat shock treated at 45°C for the indicated times. Cells were plated in 96-well plate and cell growth was monitored under real-timed cell analyzer, xCELLigence. Data were presented as the means ± S.D. of triplicated experiments (t-test; *P < 0.05, **P < 0.01).