Table 1.

Activity and lesion bypass fidelity for single amino acid mutants of human pol η

Mutant	Function/Role*	Activity**	Dark Blue plaques (%)***
			Undamaged	T-T CPD	8-oxoG
Wild Type		170 ± 38	7.1%	2.3%	29%
M14V	Active site magnesium coordination****	500 ± 140 (3.0X)	5.3%	2.2%	27%
F17L	Lid of steric gate	NA	NA	NA	NA
Q38A	Van der Waals interaction with template base	350 ± 32 (2.1X)	6.4%	7.0%	14%
Q38V	Van der Waals interaction with template base	16 ± 3 (0.1X)	6.8%	1.7%	33%
Y52E	Interaction with incoming nucleotide	120 ± 35 (0.7X)	1.4%	0.5%	3.2%
R55A	Interaction with phosphate of incoming nucleotides	ND	NA	NA	NA
R61A	Hydrogen bonds with incoming nucleotide	170 ± 20 (1.0X)	2.7%	0.9%	24%
S62A	Contact with 5′ base upstream of 1st template base	32 ± 14 (0.2X)	7.4%	2.1%	17%
S62G	Contact with 5′ base upstream of 1st template base	130 ± 20 (0.8X)	3.6%	2.8%	23%
R81C	Structure of protein	420 ± 90 (2.5X)	6.1%	4.3%	26%
E82D	Structure of protein	230 ± 87 (1.4X)	4.0%	2.1%	21%

^*Predicted function based on published reports and crystal structures

^**Picomoles of substrate extended per minute per μg protein. Values in parentheses are relative to WT. NA, not applicable. ND, none detected.

^***Frequency of dark blue plaques observed in lesion bypass assay.

^****This interaction is with the peptide bond, not the side chain.