The dynamic processivity of the T4 DNA polymerase during replication

Yang et al. 10.1073/pnas.0402625101.

Supporting Information

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Supporting Figure 6
Supporting Figure 7
Supporting Text

Supporting Figure 6

Fig. 6. Steady-state fluorescence experiment to determine the K_d between gp43 or D408N gp43 and gp45. Fluorescent donors (tryptophan) in either gp43 or D408N gp43 were excited at 290 nm, and the energy transfer to a coumarin maleimide (cpm) acceptor attached to gp45(S158C/W199F/W92F) was observed. The tryptophan donor quenching of D408N gp43 (square, solid line) or gp43 (circle, dashed line) by gp45(S158C/W199F/W92F)-cpm were used to obtain K_d values of 148 nM for gp43 and 145 nM for D408N gp43.

Supporting Figure 7

Fig. 7. Effect of [gp43] on the Okazaki fragment size synthesized on the minicircle substrate. Standard replication reactions were carried out at various gp43 concentrations in the presence of [a -³²P]dCTP to monitor the lagging strand synthesis. The average sizes of the Okazaki fragments synthesized at 240, 120, 60, 30, and 15 nM of gp43 were 1.1, 1.1, 1.0, 0.9, and 1.1 kb (lanes 1–5), respectively.