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. 2023 Mar 2;55(3):507–518. doi: 10.1038/s41588-023-01302-4

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© The Author(s) 2023

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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Fig. 4 — a, Functional enrichment of DEGs coexisting in Tifleaf3 under high temperature stress (40 °C and 35 °C) at eight time points (1–144 h; dataset A in Supplementary Table 3) and in six accessions (PI521612, PI537069, PI526529, PI583800, PI587025 and Tifleaf3) under high temperature stress (45 °C under light and 40 °C in darkness) for 1 h and 24 h (dataset B in Supplementary Table 3). b, Comparison of the proportions of upregulated ER-related and HSF genes after 1 h and 24 h of heat treatment in pearl millet, maize and rice. Heat-resistant (HR) and heat-susceptible (HS) rice samples, respectively. c, Dual luciferase assays were applied to verify that PMF0G00024.1 (RWP) could transactivate the PMA2G00107.1 (107) and PMA4G03758.1 (3758) genes. The error bars represent the mean ± s.d.; n = 3 biological replicates. Significant differences were tested using a two-tailed t-test and are shown as P values. d, Proposed activation network of pearl millet in response to growth under heat stress. After 1 h of high-temperature stress in six pearl millet accessions, many misfolded proteins activated the expression of degradation-related genes in the ER, such as genes encoding recognition proteins, including calnexin (CNX) and calreticulin (CRT), and degradation-related proteins, including heat shock proteins (HSPs), thereby correcting or degrading misfolded proteins to maintain protein homeostasis in cells. In addition, the HSF and RWP-RK genes potentially participate in this process to coregulate HSP genes.