Category:MichSt14A 36

Figrue 2: Consistent with YlqF association with the 50 S subunit, GTPase activity was stimulated in the presence of 50 S subunit, but not 30 S subunit (Fig. 2B). No activity of YlqF with the 50 S subunit-treated RNaseA was observed (Fig. 2B). Our results indicate that 50 S is indispensable for the GTPase activity of YlqF.

Figure 4: Recovered YlqF was saturated following the addition of 2-fold excess protein to the 50 S subunit, indicating that two molecules of YlqF bind a 50 S subunit (Fig. 3).

Figure 9E: AMWAP attenuates microglial migration and exerts anti-serine protease activity. Quantitative analysis of anti-protease activity in AMWAP-GFP and GFP expressing BV-2 microglia.

Figure 4: Expression of all three sigma factors is restored in the complemented strain FKO1-C (Fig. 4), confirming that a functional σF restores σE and σG expression

Figure 1E: The reporter strains expressing the Rgt1 fusions were shown to grow only in glucose-containing medium (Fig. 1E), suggesting that the Rgt1 constructs repress expression of the HXT1 promoter in the absence of glucose but negatively regulated by glucose.

Figure 3: Consistently, LexA-Rgt1 (5SA) was shown to inhibit glucose-induced expression of the reporter gene. These results suggest that the function of the LexA-Rgt1 repressor, bound to the HXT promoters constitutively, is critically regulated by its phosphorylation state.

Figure 4: the biofilm forming ability of WT showed no obvious difference upon the stimulation of glucose. Although it did not reach the level of the wild-type strain, complementation of saeRS resulted in decreased biofilm formation.

Figure 3: To verify the differentially expressed proteins regulated by SaeRS at the transcriptional level, glucose metabolism-related genes were chosen for the quantitative real-time RT-PCR analysis. The phosphate acetyltransferase transcription expression levels were significantly upregulated 1.72-fold over than those of the control.

Figure 5: Findings suggest that GreA inactivation results in the stalling of RNAP at the promoter or promoter-proximal region, supporting its general involvement in stimulation of promoter escape or suppression of promoter-proximal pausing in B. subtilis cells.

Figure 4: GreA was detected in both complexes, albeit weakly, probably due to indirect interactions. Furthermore, both NusA and σA were detected in the RNAP complex purified by using GreA-His (lane 1), supporting the association of GreA with both initiation and elongation complexes of RNAP.

Figure 3: Genome wide correlation between RNAP and GreA and NusA binding signals with correlation coefficient.

Figure 2: Based on this result we conclude that similarly to EcMccF, BaMccF likely cleaves the C-N bond in the carboxamide moiety of in DSA and ESA. Inactivations of McC by BaMccF likely occurs by the same mechanism. We therefore conclude that the MccF proteins from E. coli and B. anthracis are functionally equivalent to one another.

Figure 4: These data show that MecA and ClpC, but not ClpE, negatively affect the abundance of ComX in vivo in S. thermophilus LMD-9, confirming the above-described expression results obtained with the reporter strains.

Figure2:These results suggest that Mth1 may regulate the function of LexA-Rgt1 without directly affecting its DNA-binding ability.

Figure 4: the biofilm forming ability of WT showed no obvious difference upon the stimulation of glucose. Although it did not reach the level of the wild-type strain, complementation of saeRS resulted in decreased biofilm formation.