Figure S5. Replacement of... | Rockefeller University Press

Figure S5.

$Replacement of Asp/Glu-Lys/Arg at the end of each 12-aa repeat with Ala-Gly does not affect the MT binding of gAnkB.(A) Alignment of the 15R of human gAnkB with the sequence logo plot shown beneath. Residues at the 11th and 12th positions in the 12-aa repeats, marked by black triangles, are mutated in the ER mutant of gAnkB (15R-ER). *, :, and . indicate fully conserved, highly conserved, and conserved residues, respectively. (B) Result of a cosedimentation assay performed with 5 µM WT human gAnkB 15R and its mutant with the last two residues (Asp/Glu-Lys/Arg) of each repeat replaced with Ala-Gly (15R-ER) and Trx as the control. All of the gAnkB proteins were Trx tagged. The bands of tubulin (∼55 kD) are indicated by an arrow. gAnkB fragments and Trx bands are indicated with red boxes. The pellet fractions were quantified on the basis of band intensity and SDS-PAGE sample loading ratio (mean ± SEM; n = 3).$

Replacement of Asp/Glu-Lys/Arg at the end of each 12-aa repeat with Ala-Gly does not affect the MT binding of gAnkB. (A) Alignment of the 15R of human gAnkB with the sequence logo plot shown beneath. Residues at the 11th and 12th positions in the 12-aa repeats, marked by black triangles, are mutated in the ER mutant of gAnkB (15R-ER). *, :, and . indicate fully conserved, highly conserved, and conserved residues, respectively. (B) Result of a cosedimentation assay performed with 5 µM WT human gAnkB 15R and its mutant with the last two residues (Asp/Glu-Lys/Arg) of each repeat replaced with Ala-Gly (15R-ER) and Trx as the control. All of the gAnkB proteins were Trx tagged. The bands of tubulin (∼55 kD) are indicated by an arrow. gAnkB fragments and Trx bands are indicated with red boxes. The pellet fractions were quantified on the basis of band intensity and SDS-PAGE sample loading ratio (mean ± SEM; n = 3).