Skip Navigation

Right arrow Help viewing high resolution images
Right arrow Return to article


Table 3. {lambda}-Int and HK-Int substitution mutation phenotypes
Residue Groupa Assay resultsb Locationc Wild-type functiond Reference
Ex HJ Topo P'1 P'123 attL
WT n/a +++ + + ++ ++ ++
L80F 1 + + + ++ + – h1 {alpha}-Helix packing, dimerization 32
K93E 2a + + + ++ ++ – t1-2 H-bond DNA 32
T96I 2b – +/– – +++ +++ – h2 H-bond DNA 32
N99D 4 h2 H-bond DNA 29,31
D99A 5 + ++ ++ ++ h2 H-bond DNA 26
D99N 5 +++ +++ ++ ++ h2 H-bond DNA 26
K103 6 h2 H-bond DNA 27
I104N 1 + + + ++ + – h2 {alpha}-Helix packing 32
R108S 3 – ++ ++ – h2 Interaction surface 90, this work
P112F 1 + + + ++ + – t2-3 Turn 32
T120I 2c – + + ++ ++ – t2-3 Interaction surface 32
A125 7 h3 Interaction surface? 27
A126 7 h3 Interaction surface? 27
S139L 2b + + – + +++ +/– t3-4 H-bond DNA 32
K141 7 h4 H-bond DNA 28
R144K 2a + + – ++ ++ – h4 H-bond DNA 32
T146K 5 ++ + ++ ++ h4 {alpha}-Helix packing 26
D149R 5 + + ++ ++ h4 H-bond DNA 26
D149V 1 + + + ++ + – h4 H-bond DNA 32
E153K 1 + +* + ++ + +/– h4 {alpha}-Helix packing 32
A154T 1 – +/– – ++ + – h4 {alpha}-Helix packing 32
A154V 1 – +/– – ++ + – h4 {alpha}-Helix packing 32
G158S 1 – + + ++ + – t4-5 Turn 32
H159D 1 – + – ++ + – t4-5 {alpha}-Helix packing 32
T168N 1 + +* + ++ + – h5 {alpha}-Helix packing, dimerization 32

aThe numerical group designations are defined in Table 2. Group 2 mutants were divided into three subgroups based upon their arm-type DNA-binding activity and location within the CB domain model: (2a), no effect on arm-type binding and located proximal the core-type DNA-binding surface; (2b), enhanced arm-type binding and located proximal the core-type DNA-binding surface; (2c), no effect on arm-type binding and located distal the core-type DNA-binding surface.

bThe results of various assays are listed in columns 3–8. Results with the wild-type protein in each assay are shown in the first row. The number of ‘+’ symbols is used to indicate the level of activity measured relative to the wild-type protein in each assay. The assays and results were previously described by Han et al. (32); Ex, excisive recombination assays in vivo; HJ, Holliday junction resolution assays in vitro (the ‘+*’ symbol indicates an altered resolution bias was measured); Topo, topoisomerase activity in vitro; P'1, challenge-phage assays measuring the affinity of binding to a single P'1 arm-type site in vivo; P'123, challenge-phage assays measuring the affinity of cooperative binding to the three contiguous arm-type sites, P'1, P'2 and P'3, in vivo; attL, challenge-phage assays measuring formation of an attL intasome in vivo (see text).

cLocation: the secondary structure element containing each residue is indicated: h1, helix 1; h2, helix 2; h3, helix 3; h4, helix 4; h5, helix 5; t1–2, turn between h1 and h2; t2–3, turn between h2 and h3; t3–4, turn between h3 and h4; t4–5, turn between h4 and h5.

dWild-type function, the predicted function of the indicated residue in the wild-type protein.





Right arrow Return to article