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|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|BPT4:PORTL||DR25773, Team Purple-B||2017-04-05 10:19:34 CDT||GO:0020002 host cell plasma membrane (C)||PMID:22855489||IDA|
Figure 3: To examine the localization of the plasma-encoded gp20, researchers created a gp20 and GFP fusion protein. The gp20-GFP fusion protein and gp40, encoded by Plasmid pT20gfp-40, was transformed into E. coli BL21(DE3) cells. When analyzed using fluoromicroscopy, the researchers found that the fluorescence signal was found mostly at the cell periphery where clusters of fluorescence were observed with an apparently regular spacing between them. From this, they concluded that gp20 is membrane bound, either by itself or in an aggregated form.
|BPT4:PORTL||KY37178, Team Purple-B||2017-04-09 23:28:49 CDT||GO:0020002 host cell plasma membrane (C)||PMID:22855489||IDA|
Fig 7,Protease mapping of His-gp20 and His-gp20s, shows Both His-gp20 and His-gp20s were not digested by the protease mapping, compared with OmpA. So both proteins are most likely peripherally bound to the cytoplasmic surface of the inner membrane.
|BPP22:CAPSD||Smehr1, Team Purple-B||2017-04-17 10:24:06 CDT||GO:0046797 viral procapsid maturation (P)||PMID:26269173||IMP|
Mutant phenotypes D244A and D246A were used to show the role of the D-loop in procapsid maturation. In figure 2A, the wild type shows 2 peaks corresponding to procapsid protein around fraction 16 and mature phages that incorporated the coat protein at fraction 23. D244A mutant showed improperly formed procapsids in figure 2B which could correspond to the protein peak at fraction 16 in figure 2A. D244A showed very little coat protein at fraction 23 indicating phages were not produced. The D246A mutants showed no significant amount of procapsid protein at fraction 16. In figure 2B the D246A mutant showed particles that were incomplete instead of procapsid proteins that were present in wild types. This mutant also showed no peak of mature coat protein at fraction 23 indicating the phages were not able to form.
|BPP22:CAPSD||KY37178, Team Purple-B||2017-04-17 10:43:27 CDT||GO:0046729 viral procapsid (C)||PMID:26269173||IDA|
Figure 7. By testing disulfold crosslink form or not among purified proteins N245/C405S and L243C/C405 under room temperature and high temperature, they conclude that tips of the D-loop locates in close proximity at the 2-fold axis between coat sub-units both in capsid and precapsid. And the tips would remain in proximity after capsid expansion.
|LAMBD:RZ1||DR25773, Team Purple-B||2017-04-19 18:25:07 CDT||GO:0045861 negative regulation of proteolysis (P)||PMID:20734329||IDA|
Figure 5: Rz1 protects the C-terminal domain of Rz from proteolysis. Rz1 forms a complex that spans the entire periplasm. Researchers compared the full length of Rz with the length of Rz in the absence of Rz1. These samples were collected by rapid trichloroacetic acid (TCA) precipitation from induced cells.
|9CAUD:O56786||DR25773, Team Purple-B||2017-04-23 13:56:29 CDT||GO:0020002 host cell plasma membrane (C)||PMID:10419939||IDA|
Figure 5: Hol187 is found in the cytoplasmic membrane of phage-infected cells. Immunoblotting with specific peptide antibodies against Hol187 showed Hol187 is synthesized in S. aureus host cells when infected with phage 187. Immunoblotting enabled the detection of Hol187 in membrane fractions of these cells. Uninfected control cells did not have a signal.
|9CAUD:O48503||KY37178, Team Purple-B||2017-04-23 22:59:28 CDT||GO:0098689 latency-replication decision (P)||PMID:27258092||IMP|
Figure 1 and Table 1 show mutant on different part of CI binding site< right before the site, on the site, or right after the site, would cause clear plaques or not.