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. Author manuscript; available in PMC: 2020 Oct 3.
Published in final edited form as: Mol Cell. 2019 Aug 14;76(1):177–190.e5. doi: 10.1016/j.molcel.2019.06.044

Figure 2. The ARF19 PB1 domain and middle region (MR) are required for protein assembly formation.

Figure 2

(A)Cartoon depictions of examined YFP-tagged ARF19 variants and truncations.

(B) ARF19 PB1 domain homology model with the negative (red) and positive (blue) halves of each indicated. Lys962 is at the interface on the positive face and is surrounded by a cluster of negatively charged residues from the opposing domain (Asp1012, Glu1014, Asp1022). The filamentous asymmetric unit from PDB entry 4NJ6 was used to construct a putative macromolecular filament through repetitive addition.

(C) Fluorescence microscopy images from the upper root regions of 5d-old UBQ10:YFP-ARF19, UBQ10:YFP-ARF19K962A, UBQ10:YFP-ARF19PB1, and UBQ10:YFP-ARF19MR+PB1 Arabidopsis seedlings.

(D) Quantification of ARF oligomeric state in upper root and root tip sections of ARF proteins in nuclei or condensates (n ≥ 10).

(E) Representative N&B analysis of an image of a YFP-ARF19 condensate from the upper root. Black represents background fluorescence, gray monomer, blue dimmer, green 3–10mer, and yellow >10mer. ND: not detected.