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. 2023 Apr 13;14:2104. doi: 10.1038/s41467-023-37660-0

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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. 2 — a V. cholerae biofilms expressing mScarlet-I (Top) incubated with 1 μM purified and GFP-tagged proteins (Bottom) with the indicated domain(s). The VPS⁻ control was performed with ΔvpsL cells unable to produce VPS. b Cross-sectional images (at z = 6 μm) of biofilms from cells expressing wild-type Bap1 (Left) and Bap1_ΔVelcro (Right), both tagged with a 3×FLAG tag at the C-terminus and stained with an anti-FLAG antibody conjugated to Cy3. Inset: magnified image of the region highlighted by the white box, with the cell signal (mNeonGreen) overlaid with Cy3. c EMSA images showing the binding of purified Bap1’s β-propeller to purified VPS. Red arrows = protein-VPS complex, black arrows = unbound proteins, green arrows = free GFP. See Supplementary Fig. 2i for positive control and results from RbmC’s β-propeller. When present, the protein amount in a lane is 5 µg. The VPS amount is 0, 0.0625, 0.125, 0.25, 0.50, 1, 5, 5, 5 µg in each lane from left to right.