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. 2021 Jan 29;11:2692. doi: 10.1038/s41598-021-82164-w

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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The Bromo domain of KAP1 promotes Tat degradation via the proteasome pathway (A,B,E,F) HEK cells were transfected with the indicated vectors. 48 h later, the nuclear proteins were analyzed by Western blot for the presence of the indicated proteins. (B) Tat expression level whose relative quantification to the α-tubulin was carried out using the image J software. (C) The RNA extracts from HEK cells transfected with the indicated plasmids were submitted to RT-qPCR experiments against Tat. The relative mRNA level of Tat was normalized to the GAPDH gene. (D) HEK cells were transfected with the indicated vectors. After 18 h of transfection, the cells were treated or not with 50 μM of MG132 for 6 h. 24 h post-transfection, the total protein extracts were analyzed by Western blot for the presence of KAP1 and Tat. Tat expression level was quantified relatively to β-actin expression, using image J software. A t-test was performed on 3 (B,C) and 5 (D) independent experiments P (*P < 0.05, **P < 0.01, ***P < 0.001). Full-length blots are presented in Supplementary Figure 7.