Skip to main content
. Author manuscript; available in PMC: 2016 Jun 18.
Published in final edited form as: ACS Chem Biol. 2015 Oct 15;10(12):2672–2679. doi: 10.1021/acschembio.5b00765

Figure 1.

Figure 1

Hsp104 potentiation. Diverse missense mutations in disparate positions throughout the MD and small domain of NBD1 potentiate Hsp104. (A) Δhsp104 yeasts integrated with genes encoding TDP-43, FUS, or α-synuclein were transformed with the indicated Hsp104 missense mutants or control. Strains were serially diluted 5-fold and spotted on glucose (off) or galactose (on) media. (B) Selected strains from A were induced for 5 h, lysed, and immunoblotted. 3-Phosphoglycerate kinase (PGK) serves as a loading control. (C) Potentiating mutations are distributed throughout the MD of Hsp104. The MD (green, residues 411–538) is comprised of four helices and is inserted into nucleotide-binding domain 1 (NBD1, blue). Potentiating mutations shown in this figure are further described in this paper and our earlier work.17 (D) Homology model of the MD and a portion of the small domain of NBD1 of Hsp104, where side chains studied are shown as sticks. Residues where the tested mutations potentiate Hsp104 are shown in green and are numbered. Residues where the tested mutations do not potentiate Hsp104 are shown in red.