Category:Team Las Transposones

Mutant Phenotype was deduced based on Table 3: Impact of LytF on the efficiency of gene transfer from donor to recipient cells during co-cultivation. The table strongly indicates that LytF causes lysis of AH2 target cells (hydrolase activity), followed by release of DNA that can be taken up by competent SGH25 cells.

Mutant Phenotype was inferred based on Figure 1: Detection of in vivo phosphorylated proteins in S. pneumoniae. Cell lysates from cultures of a wild-type strain of S. pneumoniae (Sp1) and a ΔstkP mutant strain (Sp10) were immuno-labeled and the patterns of phosphorylated proteins in the cytoplasmic and membrane fractions were compared.

The anti-pThr antibody reacted with at least six protein bands in the wild type; however, no phosphorylated proteins were detected in the Sp10 strain. This result indicated that phosphorylation on Thr residues in S. pneumoniae is dependent on the presence of StkP.

Mutant phenotype was inferred based on Figure 4, in which SpyA was assayed for the ability to ADP-ribosylate arginine.

As shown, there was labelled precipitated material when SpyA was incubated with poly-l-arginine and only limited precipitated radioactive material with the active site mutant SpyA-E187A.

Figure 4 shows the Lineweaver–Burk plot representation of the LdRpiB kinetics data. Recombinant Ld RpiB activity was assayed in the presence of different concentrations of ribose 5-phosphate (R5P)

Table 2 shows data from the Lineweaver- Burk plot analysis of this enzyme preparation, in order to test substrate specificity. 4-methylcatechol was the most suitable substrate for this enzyme

Figure 6 shows the lytic activity of the lysozyme purified from tick gut; using a zone assay with M. luteus. Moreover, Fig. 7 displays the determination of pH optimum of the tick gut lysozyme and its comparison with egg lysozyme.

Figure 4 shows the activity of recombinant HILysozyme, that was performed using Micrococcus lysodeikticus powder as a substrate. It is shown that the diameter of the clear zone depends on the protein concentration. This effect is similar to the effect caused by the egg white lysozyme used as control. (Although this data were not shown)

Figures 4 shows the Acyltransferase activity measured by the transfer of [1-14C]acyl-CoAs or [3H]acetyl-CoA to lysophospholipids to form phospholipids. The lysophospholipid preferences of mLPAAT3 were determined. The substrate specificity of the mLPAAT3 enzyme was measure using [1-14C]arachidonoyl-CoA as an acyl donor, and using a variety of lysophospholipid acceptors.

Direct Assay Evidence Code was inferred based on Figure 3: SDS-PAGE (left) and fibrin zymogram (right) of culture supernatant, which shows bands of 90, 55, and 40 kDa of B. subtilis TF (cells harboring pHYbpr86-1) that were likely derived from bacillopeptidse F.

Table 2 shows the formation of arginine decarboxylase (ADC) by the wild-type strain and the speA mutants under different growth conditions. Spe A mutant had lower levels of ADC.

Table 2 shows the formation of ornithine decarboxylase (ODC) by the wild-type strain and the speC mutants under different growth conditions. Spe C mutants had lower levels of ODC.

IMP based on Fig. 2 and Figure 3 evidence; Figure 2 shows the production of an extracellular signalling molecule with AI-2-like activity by C. jejuni NCTC 11168; Figure 3 shows that Cj1198 can generate AI-2-like activity in a heterologous host when the addition of cell-free culture medium from cells containing pKE25 stimulated luminescence in a manner similar to the positive control (V. harveyi BB152).

IDA based on Figure 2 evidence, in which a recombinant soluble form of PpiA that had been produced and secreted in L. lactis and purified from a culture supernatant displayed both PPIase and chaperone activities.

IMP was conclude based on Figure 3, which indicates XerS/difSL Recombination in E. coli. In absence of the lactococcal XerS recombinase, almost no recombination was observed indicating that XerCD of E. coli do not recombine difSL. In contrast, introduction of a plasmid expressing the lactococcal xerS gene increased the excision frequency (observed in E. coli when using the native XerCD/dif system.)

IMP was demonstrated based on Figure 2, which shows autolysin profile of wild type and complementation strain. The lytic pattern was absent in the mutant strain.

Figure 7 and 9 show degradation of the lamba O protein by the ClpXP protease, being completely dependent on the presence of ATP, whereas table IV shows results for several nucleotides tested as energy source. The data demonstrated the ATP specificity of this protease.

Figure 3 shows the expression profile of aguBA strain with different carbon and nitrogen sources. The agmatine deiminase activity (AguA) was induced in media containing agmatine. Table 2 shows these data as well; but displaying that in the mutant of the repressor operon, the enzyme was constitutively expressed.

IDA based on evidence showed on Fig. 4.

Cloning of the LevH1 enzyme catalytic region in E. coli XL1. Different protein profiles were constructed based on LevH1 gene. The enzymatic activity of the pKNL1 recombinant plasmid suggests that both, variable and catalytic domains, are essential for LevH1 inulinase activity.

IDA is supported by Fig 5. Overexpression of esterase from Lactobacillus casei CL96 in E. coli BL21(DE3)/pLysS. A polypeptide with a molecular mass of about 68 kDa and esterase activity was produced, in agreement with

the calculated molecular mass of the predicted amino acid sequence.