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Category:Team Drexel 17A
|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|BPT4:D9IE49||MNatrajan, Team Drexel 17A||2017-04-12 10:28:52 CDT||GO:0061157 mRNA destabilization (P)||PMID:26323881||IMP|
Figure 2 Shows the role of Srd in destabilizing lpp and ompA mRNAs by inhibiting Srd by adding rifampicin and by activating expression of Srd by adding arabinose.
|CVHNL:SPIKE||Kvieira, Team Drexel 17A||2017-04-13 11:41:20 CDT||GO:0019062 virion attachment to host cell (P)||PMID:21798295||IMP|
Figures 3c and d show that high expression levels on cell surface are positively correlated with high S protein levels in the virion, therefore, showing this protein helps with attachment/infection.
|BPT4:UVSW||MNatrajan, Team Drexel 17A||2017-04-19 09:18:00 CDT||GO:0009379 Holliday junction helicase complex (C)||PMID:17823128||IMP|
Figure 5: In the presence of ATP and wild type UvsW branch migration of DHJS-2 Holliday junction occurs, whereas branch migration does not occur in the presence of K141R mutant of UvsW and even in the presence of UvsW when ATP is absent.
|VIBCH:TCPB||Kvieira, Team Drexel 17A||2017-04-20 11:33:53 CDT||GO:0009297 pilus assembly (P)||PMID:27992883||IMP|
Figure 2A shows reduction of TCP bundles in the mutant V. cholerae with a deletion of the TcpB gene compared to the wild type that has extensive TCP bundles.
|BPPH2:PKG16||Kvieira, Team Drexel 17A||2017-04-25 15:40:16 CDT||GO:0019073 viral DNA genome packaging (P)||other:PMC60195||IDA|
Figure 2 shows that packaged DNA could only be extracted when all components of the packaging system, including p16, were present. Lone RNA, DNA terminal protein, or p16 did not produce packaged DNA. (this article is from pubmed but there was no PMID available.)
|BPT5:PRO||Kvieira, Team Drexel 17A||2017-04-27 11:54:45 CDT||GO:0019069 viral capsid assembly (P)||PMID:26616586||IMP|
Mixture of pb11 affected the migration of pb8p (Fig 3a) so pb11 interacts with pb8p; this interaction induces production of prohead like particles (Fig 3b). Experiments reveal that light scattering increases with higher pb11 concentration because of the density of the formed capsid and tube particles (Fig 4a, 4c, 4d). Also shown is pb8p amount being inversely proportional to pb11 amount (Fig 4b) supporting pb11 interaction and capsid assembly role.
|BPDPK:Q8SDD3||Kvieira, Team Drexel 17A||2017-04-27 12:21:08 CDT||GO:0098027 virus tail, sheath (C)||PMID:19822340||IDA|
Electron microscopy revealed no gold particles (antibodies) in the control but revealed particles on the tail sheaths of the sample (Fig 4a, 4b) concluding that the protein is located on the tail sheath.
|STAAU:A0A0U1MKT4||Kvieira, Team Drexel 17A||2017-05-16 12:13:50 CDT||GO:1990814 DNA/DNA annealing activity (F)||PMID:28475766||IDA|
Figure 1A shows the recombinase, 80α Sak, having affinity for ssDNA as opposed to Figure 2 which shows reduced affinity for dsDNA. 80α Sak's ssDNA annealing activity is shown in Figure 3A's electrophoretic shift assays where an increased amount of annealed ssDNAs was produced in the ssDNA aliquots mixed with 80α Sak protein when the time incubation increased.
|BPP22:VG08||Kvieira, Team Drexel 17A||2017-05-23 11:46:28 CDT||GO:0046797 viral procapsid maturation (P)||PMID:22879595||IMP|
In figure 2a, the activity of scaffolding protein and mutations is measured via light scattering, and the results show greatly decreased activity compared to the wild type. Figure 2b compares procapsid assembly in wild type and mutated scaffolding proteins via NaCl affinity experiments. While the wild type formed more procapsids with increasing NaCl concentration because "fewer nuclei are formed and reactants are not exhausted, so that complete PCs[procapsids]form," the mutants resulted in decreased procapsid assembly.
|BPPH6:RDRP||Kvieira, Team Drexel 17A||2017-05-23 12:22:38 CDT||GO:0039696 RNA-templated viral transcription (P)||PMID:11080173||IDA|
Figure 2b shows dsRNA formation proportional to P2 polymerase concentration(lanes 3-6). Also, no dsRNA was found when P2 polymerase was substituted with bovine serum albumin (lane 2).
|PSEAE:G3XD04||Kvieira, Team Drexel 17A||2017-05-30 11:48:29 CDT||GO:0006289 nucleotide-excision repair (P)||PMID:27303696||IMP|
Figure 2 shows two tests supporting UvrD's role in nucleotide excision repair. The first, 2A, shows how the mutant lacking UvrD generated more rifampin-resistant cells as a result of a defective DNA repair system. Then in 2b, cells lacking the UvrD protein had less chance of survival due to increased vulnerability to UV, which is known to cause DNA mutations. Therefore, the UvrD mutants had no repair system to fix the UV mutations.