TABLE 3.

Quantitative analysis of in vitro DNA binding by Swi5 mutants^a

Swi5 protein	Class	% Of complex formed by protein at HO DNA
		Binary complex without Pho2	Ternary complex with Pho2
Wild type		17	100
E482K mutant	B	15	67
S483G mutant	B	20	70
R484G mutant	C	20	89
Wild type		18	100
R484S mutant	C	22	107
F485S mutant	B	17	67
V494A mutant	C	20	112
Wild type		12	100
S497P mutant	A	12	6
Q498R mutant	A	12	16
S505P mutant	C	10	82

^aThe amounts of DNA bound in Swi5-DNA and Swi5-Pho2-DNA complexes were quantitated, as described in Materials and Methods, from the gel retardation assays shown in Fig. 4. The amount of Swi5-Pho2-DNA complex formed by using wild-type Swi5 was normalized to 100% in each experiment, and the relative fraction of complex formed by the Swi5 mutants was calculated accordingly. The amount of Swi5-DNA binary complex formed was similarly normalized to the amount of the wild-type Swi5-Pho2-DNA ternary complexes.