Fig. 1: Type A/B PB1 domains and their capability to form polymers.
From: Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
a Sequence alignment of the type A/B PB1 domains with highlighted tandem arginine motif (blue) in addition to basic (blue) and acidic residues (red). b Domain architecture of PKCz, TFG1, p62, and AtNBR1 proteins. c Pelletation assay of purified type A, B, or AB PB1 domains: TFG1, AtNBR1, PKCζ, p621–102, and p621–122. Corresponding lanes of soluble (S) and pellet (P) fraction are shown. Only PKCζ remains soluble, whereas TFG1, AtNBR1, and p62 are found in the pellet. Source data are provided as a Source Data file. d Electron micrographs of negatively stained specimens reveal elongated filamentous p621–122, tubular polymers of TFG1 and AtNBR1 of 145 ± 5, 900 ± 52, and 120 ± 4 Å nm in diameter, respectively.
