|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|BPPH2:PKG16||Bhorne1, Team Blue-A||2017-04-07 19:36:59 CDT||GO:0019073 viral DNA genome packaging (P)||PMID:16376938||IDA|
Figures 5 & 6 show binding of gp16 to the procapsid-pRNA complex in vitro, much more so that to procapsid alone, confirming the synergistic role of gp16 and pRNA in the translocation of DNA into the viral procapsid.
|BPSPP:Q38072||Amrutha2, Team Blue-A||2017-04-09 21:45:58 CDT||GO:0008821 crossover junction endodeoxyribonuclease activity (F)||PMID:23119018||IDA|
Authors use AFM and Western blotting to analyze the product of gene 44, referred to as G44P, and how it binds to Holliday junction (HJ) structures (Figure 5) then cleaves 1-2 bp away from both static and mobile HJs (Figure 6).
|BPPH2:GP13||Bhorne1, Team Blue-A||2017-04-09 23:18:01 CDT||GO:0098004 virus tail fiber assembly (P)||PMID:18394643||IDA|
GP13 is seen as structural component of the phage ϕ29 tail. Figure 2, uses Western Blot Analysis to infer that gp13 is a component of the tail fiber. Loss of gp13 causes the tail tip, results in a shortened tail (missing tail fibers) . This is specified in Table 3, which quantifies assembly of WT and several gp 13 mutants.
|BPT5:HEL10||Bcarty1, Team Blue-A||2017-04-10 13:53:04 CDT||GO:1990163 ATP-dependent four-way junction helicase activity (F)||PMID:28009009||IDA|
The authors use a ATPase assay to determine if the helicase D10 can unwind complex branched DNA substrates. Figure 2b shows the ATP dependent unwinding of cruciform (four-way junction) DNA molecules by the T5 helicase gene D10.