The ΔrelA Y. pestis mutant was as virulent as wild type Y. pestis KIM5+ (Fig. 6), while the ΔrelA ΔspoT Y. pestis mutant was dramatically attenuated.
However, sporulation of this mutant was dramatically reduced in the presence of high calcium concentrations, suggesting that certain proteins engaged in sporulation require N-glycan outer chains to be fully functional.
In contrast, the NEECK mutant was dramatically slower, with t1/2 >6,134 s.
Though rec12Δ mutants also form dyads (Fig. 2A) (Davis and Smith, 2003), the level of dyad formation of the dfp1-35 mutant is dramatically higher than that in the rec12Δ cells.
The projection profile of the Y7.53F mutant is dramatically different from that of the WT with 77.2% of the conformations in the negative direction.
We found that whereas loss of either set1 or clr3 resulted in increased levels of siRNAs, the siRNA level in the set1Δ clr3Δ double mutant was dramatically diminished relative to wild-type.
Although the growth of Δ pkaA mutant was dramatically reduced in liquid glucose-containing minimal media (data not shown), the growth rate was comparable to the wild-type strain when grown in liquid complete YG media (24 h, wild type = 0.116 ± 0.010 g/10 conidia; Δ pkaA = 0.167 ± 0.1018 g/10 conidia).
However, thermal hysteresis activities of several mutants were dramatically reduced (Figure 7, Table S3 and Table 2).
Contrary to this idea, the evoked EPSC and endogenous EPSC defects observed in unc-13 [L−S+] mutants were dramatically stronger than in UNC-13S rescue, but were slightly less severe than in unc-13 s69 unc-13 s69consistent with prior studies (Richmutants al., 1999).
The affinity of SU 1-30 for all of W394 mutants was dramatically reduced, while the other mutants bound similarly to wild type SU, indicating that W394 is a key residue for the epitope recognized by SU 1-30 (Table 4).
