Research Article

The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster

Figure 2

N-terminal domain of Rtel1 (RtelN) contains an iron-sulfur cluster. (a) UV-visible absorption spectrum of purified RtelN. Purified RtelN (30 μM) was dissolved in buffer containing Tris (20 mM, pH 8.0) and NaCl (500 mM). The absorption peak at 415 nm indicates an iron-sulfur cluster in RtelN. Inset is a photograph of cell pellets after induction with (sample 2) or without (sample 1) IPTG (200 μM). (b) Circular dichroism (CD) spectrum of purified RtelN. Purified RtelN (6.75 μM) was dissolved in potassium phosphate buffer (10 mM, pH 8.0). The spectrum was an average of three scans. Insert is a photograph of the SDS-PAGE gel of purified RtelN. Left lane, molecular marker (M); right lane, purified RtelN.
285791.fig.002a
(a)
285791.fig.002b
(b)