Category:Team Skinny Genes

Figure 1

These results (Fig. 1 and Table 1) show that E. coli umpA mutants (strains SK634, SK635, and SK636) were defective in diacylglyceryl modification of prolipoprotein because of defective diacylglyceryl transferase. Defective modification of prolipoprotein in umpA mutants was confirmed by in vitro analysis of prolipoprotein modification activity.

in Table 3 are the mutant DNA strains (dnaE486 and dnaE511) against the wildtype to show that the increasing mutations are caused by defects in the DNA polymerase III alpha subunit that are encoded by dnaE. The mutations of the dnaE prove to be responsible/involved in DNA polymerase activity.

The expression of traJ was activated at low concentration of bile salts and decreased with increasing bile salt concentration. The expression patterns of traJ were corresponded with the conjugative transfer frequencies between S. typhimurium and e. coli.

Figure 2 A and D: they show both the wild type and the double mutant Wnt5a -/-;Wnt11-/-. It can also be seen in figure 2 B and C that the single mutants do not fully develop the ventricular septum

Table 2 shows strain 577, which carries the end-14 mutation, is deficient in the major endonuclease

Both SbcC and SbcD polypeptides are required for the ATP-dependent double-strand exonuclease activity of SbcCD (Fig.3b) only the SbcD polypeptide is required for the ATP-independent single-strand endonuclease activity of SbcCD

Figure 1. shows the effect of the Id1 protein on endothelial progenitor cells proliferation and migration using RT-PCR, Western blotting, and MTT assay.

Figure 1. shows the role of LOX-1 in atherosclerosis. OxLDL binds to LOX-1 on the endothelial cell surface triggering activation of an inflammatory reaction.

Figure 1A. and 1B, KiaABC complex help regulate the circadian rhythms by gene expressing of wild type compared to a null mutant.

As shown in Table 3, the wildtype strain of the gene sbcB shows exonuclease activity. When the anitserum, that inhibits exonuclease activity, was added the exonuclease activity decreased proving the exonuclease activity of the crude lysates. To verify the sbcB gene activity, the gene was mutated, sbcB15 and when mutated the exonuclease activity decreased to show that the sbcB gene is responsible for exonuclease activity.

Figure 1F. shows, using digital fluorescence microscopy, that Vav3 translocates to the plasma membrane and localizes to the immunological synapse upon T cell activation.

Immunohistochemical analysis of BAG3 expression in Figure 1 A, E and F.

Figure #1, western blot and TUNEL assay.