Figure S1 - Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensis

Sequence alignment of the ClpB sequences from Ehrlichia chaffeensis, Escherichia coli, Thermus thermophilus, Saccharomyces cerevisiae, and Arabidopsis thaliana. Structural domains: N-terminal domain (ND), linker, D1, middle domain (MD), and D2 are indicated below the alignment in bold typeface. The domains’ borders were obtained from the crystallographic data for T. thermophilus ClpB [Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, et al. (2003) The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115∶229–240]. The characteristic motifs of AAA+ ATPases are indicated below the alignment in italics. (PDF)