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Figure 5


Fig. 5. A point mutation in the ATP-binding domain of UAP56 inhibits ATP binding. A Lysine 95 to Asparagine mutation in the ATP-binding domain of GST-UAP56 was made. Using a method applied to previous DEAD-box helicases (Pause and Sonenberg, 1992), GST-UAP56 wt or GST-UAP56 K95N was UV-cross-linked to bound {alpha}-P32-ATP in the presence or absence of 0.1 OD260 units of polyU. The bound and unbound {alpha}-P32-ATP were separated on a 12% SDS-PAGE gel before phosphoimaging. The binding of {alpha}-P32-ATP was strongly reduced by the mutation but unaffected by polyU.





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