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. 2023 Jan 24;14:378. doi: 10.1038/s41467-023-36063-5

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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. 3 — a Fluorescence images showing liquid droplets of EGFP-NUT (residues 300–700) with increasing amounts of the protein as indicated. Histogram plots showing total area of droplets per field (36 × 36 μm). Scalar bars: 5 μm. Quantitative data (right) are shown as mean +/− S.D. (n = minimum of three independent samples for each condition). p-values for each indicated comparison are two-tailed unpaired and derived from Student’s t-test without adjustment for multiple comparisons. b Microscopic images depicting EGFP-NUT (residues 300–700, 2.5 μM) droplet formation at different salt concentrations as indicated. Scalar bars: 5 μm. Quantitative data (right) are shown as mean +/− S.D. (n = minimum of three independent samples for each condition). p-values for each indicated comparison are two-tailed unpaired and derived from Student’s t-test without adjustment for multiple comparisons. c Images showing fusion (top) or fission (bottom) of EGFP-NUT (residues 300–700, 2.5 μM) droplets in a time course as indicated. Scalar bars: 1 μm. Experiments were repeated at least twice. d Fluorescence images showing liquid droplets of EGFP-NUT (residues 300–700, 2.5 μM) with addition of Cherry-TAZ2 as indicated. Histogram plots showing total droplet areas per field (36 × 36 μm) in different NUT to TAZ2 molar ratio. Three fields are quantified. Scalar bars: 5 μm. Quantitative data are shown as mean +/− S.D. (n = minimum of four independent samples for each condition). p-values for each indicated comparison are two-tailed unpaired and derived from Student’s t-test without adjustment for multiple comparisons. e Supernatant (S) and pelleted (P) fractions from droplet spin down experiments were run in western blots to assess the time-dependent (0–24 h of phase separation) formation of heat-, reducing- and SDS-stable EGFP-NUT/Cherry-TAZ2 oligomers. Note that some high molecular weight protein complexes (HMW multimers) appeared shortly after addition of Cherry-TAZ2. Data represent mean +/− SEM from three independent experiments. p-values for each indicated comparison are two-tailed unpaired and derived from Student’s t-test without adjustment for multiple comparisons.