Table 1.
Activities of wild-type and mutant forms of gp45
| gp45 species | ATPase, nM s−1*
|
||
|---|---|---|---|
| gp45 and gp44/62 | gp45, gp44/62, and DNA | gp45, gp44/62, DNA, and gp43 | |
| Wild type | 19 | 303 | 23 |
| S158C/W199F | 13 | 316 | 17 |
| S158C/W199F-CPM | 12 | 101 | 12 |
| T168C/W199F | 19 | 263 | 27 |
| T168C/W199F-CPM | 19 | 318 | 45 |
| W92F/S158C/W199F | 25 | 297 | 28 |
| W92F/S158C/W199F-CPM | 23 | 196 | 26 |
| W92F/T168C/W199F | 22 | 304 | 35 |
| W92F/T168C/W199F-CPM | 14 | 266 | 28 |
*
Verification of the ability of the mutants to simulate ATPase activity in the presence of DNA. Shutdown rates of ATPase activity with the addition of gp43 were very close to the basal rate with gp45 and gp44/62 alone. The ability to stimulate and shut down ATPase activity is a sufficient test for the formation of a functional holoenzyme. Experimental error and reproducibility is 10%.