Category:Team Anonymous

Figure 2B shows that cells with a mutant CAC2 gene produced more 4N cells than the wild type. Figure 2C shows these 4N cells were due to abnormal nuclear localization, or an abnormality in chromosome segregation. This indicates that CAC2 is needed for proper chromosome segregation.

Figure 2B shows that cells with a mutant HIR1 gene produced more 4N cells than the wild type. Figure 2C shows these 4N cells were due to abnormal nuclear localization, or an abnormality in chromosome segregation. This indicates that HIR1 is needed for proper chromosome segregation.

Figure two shows that the cysteine protease inhibitor, originally located in the cytoplasm, localizes to the lysosome during cyst formation.

Figure 1B and 1C show that the cysteine protease inhibitor inhibited human cathepsin L, human cathepsin B, and papain enzymes. All of these enzymes are part of the C1 family of cysteine proteinases, therefore showing that the cysteine protease inhibitor inhibits protease, or peptidase, activity.

Figure 2 shows that mature hyphae lacking Rsr1 had an Spk intensity index that was much less than the wild type index. Spk is known to be needed for hyphal morphogenesis. Mature hyphae lacking Rsr1 had lower Spk intensity than germ tubes lacking Rsr1, showing that Spk decreases over time without Rsr1. Figure 3 shows strains lacking Rsr1 had decreased localization of Mlc1- YFP in the tips when compared to the wild type. Figure 4A shows the overall defects in morphogenesis of organisms lacking Rsr1 compared to the wild type, including wider cells. Figure 5 shows that Rsr1 focuses Cdc42 activity at the tips of germ tubes and is required to maintain polarized growth needed for development. All of these figures show that Rsr1 interacts and regulates Spk vesicles and its components leading to the establishment of cell polarity.

Figure one shows that Gadd-45 arrests human fibroblasts in the G2/M cell cycle phase.

Figure 3 shows that overexpression of the ribosomal protein S7 resulted in overproduced expression of GADD45alpha, a known cell checkpoint protein. Therefore the S7 ribosomal protein helps to regulate cell cycle checkpoints.

Table 2 shows that mice injected with LLO died due to hemolysis. However, when cholesterol, heat, or N-ethylmaleimide blocked the LLO activity the mice lived.

Figure 3 shows that control tobacco plants had a 100% change of C180160 values, while tobacco plants with mutants that produced significantly lower levels of carbonic anhydrase only had a 20% change. Therefore carbonic anhydrase must be involved in the carbonate dehydratase activity.

Figure 3 shows that cells containing mutant p35 undergo DNA fragmentation, suggesting apoptosis. However, wild type cells with an intact p35 did not undergo apoptosis as the DNA did not fragmentize. Figure 2 also shows apoptotic characteristics such as blebbing for the vAcAnh mutant. This mutant maps to the p35 gene.

Different substitutions in the residues of the H protein are shown in figure 5A. While the wild type and some mutant H proteins produced syncytia, some mutants failed to produce syncytia, showing that these residues are important for the function of the H protein, which is to perform syncytia by cell fusion. Figure 4 also shows the cell-to-cell fusion properties of the H protein.

Figure 4B shows that HtpR was needed to successfully transcribe from the P1 and P2 promoter of DnaK. DNA was required for this transcription, therefore showing that HtpR is involved in DNA-dependent transcription.

E.coli with a deleted recA and one lacZ gene on a chromosome and one lacZ gene on a plasmid were used. The lacZ genes being on different alleles caused the E.coli phenotype to be Lac-. When a plasmid containing Synechococcus sp. strain PCC 7002's recA gene were introduced into E.coli some E.coli became Lac+ showing that the synechococcus recA gene functions in DNA recombination. These results are shown in Table 2.

Figure four shows that the core RNA polymerase by itself cannot transcribe from the heat shock promoter without HtpR. However, when just HtpR is added to the core RNA polymerase it can transcribe from the heat shock promoter, indicating that HtpR is a sigma factor and binds RNA polymerase and effects its transcription activity.