Sentence examples for mediate heme repression from inspiring English sources

To better understand how this regulation occurs, we tested mutants lacking one or both of the known outer membrane heme receptors for their ability to mediate heme repression of PrrH.

Furthermore, they demonstrate that heme repression of PrrH is mediated by a regulatory mechanism that is distinct from heme-dependent regulation of the PrrF RNAs.

These data indicate that heme repression of PrrH is dependent on the entire heme moiety and distinguish heme regulation of the PrrH RNA from Fur-mediated iron regulation of the PrrF RNAs.

Residual heme repression of PrrH in the ΔphuRΔhasR mutant, albeit statistically insignificant (P>0.2 by student's t test), could be mediated by a third putative heme outer membrane receptor encoded by PA1302; work is currently underway to determine the role of this gene in heme uptake and regulation.

Indeed, loss of the HemO heme oxygenase in a ΔhemO mutant reduced repression of PrrF by heme (Figure 3E), while, in contrast, causing a slight increase in heme repression of PrrH (Figure 3D).

While loss of either PhuR or HasR alone had no effect on heme repression of PrrH, deletion of both heme receptors caused a small increase in PrrH expression in the presence of heme (Figure 6A).

In fact, loss of PhuR alone nearly eliminated heme repression of PrrF, and loss of both the PhuR and HasR heme receptors ablated the ability of heme to affect PrrF expression (Figure 6B).

Residual heme repression of PrrF expression in the ΔhemO mutant is likely due to overlapping detection of the PrrH RNA by this primer-probe set, as well as effects from contaminating iron in the heme preparation.

P. aeruginosa encodes for a putative ECF sigma factor and transmembrane sensor adjacent to the hasR gene, encoding one of the heme outer membrane receptors important for heme repression of PrrH.

Among the Isd genes that mediate heme uptake, only isdD (a heme ABC transporter) was consistently upregulated in vivo and only versus logarithmic phase S. aureus.

This ΔhtsAΔisdE mutant is functionally inactivated for both Isd and Hts-mediated heme transport.