CELL BIOLOGY. For the article “The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations,” by Sharon Cantor, Ronny Drapkin, Fan Zhang, Yafang Lin, Juliana Han, Sushmita Pamidi, and David M. Livingston, which appeared in issue 8, February 24, 2004, of Proc. Natl. Acad. Sci. USA (101, 2357-2362; first published February 17, 2004; 10.1073/pnas.0308717101), the authors note that the x axis of the left graph in Fig. 2B is numbered incorrectly. The corrected figure and its legend appear below.
Fig. 2.
BACH1 is an ATP-dependent helicase. (A) Increasing amounts of WT and K52R mutant BACH1 were incubated with a DNA helicase substrate containing an annealed radiolabeled 19-nt oligomer (see Materials and Methods). Lane 1, annealed substrate (-); lane 2, heat-denatured substrate (B, for boiled); lanes 3-5, BACH1 (60, 180, and 450 ng, respectively); lanes 6-8, K52R BACH1 (200, 400, and 600 ng, respectively); lane 9, WT with no ATP. (B) BACH1 unwinds DNA in a time- and dose-dependent manner. BACH1 protein (150 ng) was incubated with the 19-mer helicase substrate for the indicated times. Independently, increasing amounts of BACH1 (15, 30, 60, 120, 240, and 480 ng) were incubated with substrate for 30 min. (C) Increasing amounts of BACH1 (60, 180, and 450 ng) were incubated with a RNA:DNA helicase substrate and helicase activity was measured. (D) Increasing quantities of BACH1 (60, 180, and 450 ng) were incubated with DNA helicase substrates of increasing partial duplex length, as indicated. In all cases, reaction products were resolved in an 8% native polyacrylamide gel containing 15% glycerol. Results were quantitated by using a Molecular Dynamics STORM PhosphorImager.