GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
Phage Hunters Spring 2016
|Status||Page||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|BPT7:GP73||2016-04-18 06:00:55 CDT||GO:0019012 virion (C)||PMID:16054667||ECO:0000315 mutant phenotype evidence used in manual assertion|
|BPT7:GP67||2016-04-18 06:06:39 CDT||GO:0039620 T=7 icosahedral viral capsid (C)||PMID:16054667||ECO:0000315 mutant phenotype evidence used in manual assertion|
|BPT7:CAPSA||2016-04-26 12:30:01 CDT||GO:0098017 viral capsid, major subunit (C)||PMID:20962334||ECO:0000314 direct assay evidence used in manual assertion|
Figure 2A: Researchers purified T7 virions from E.coli cells and separated the viral heads. Cryo-electron microscopy was used to examine the empty viral heads, and the structure of gp10A was determined to be that of a T=7 icosahedral capsid, major subunit.
|BPT7:GP04||2016-04-26 21:27:53 CDT||GO:0044865 negative regulation by virus of host cell division (P)||PMID:24218612||ECO:0000314 direct assay evidence used in manual assertion|
|BPT7:DNBI||2016-05-01 19:40:34 CDT||GO:0003674 molecular_function (F)||PMID:1634538||ECO:0000314 direct assay evidence used in manual assertion|
Figure 3: A nitrocellulose filter was used to determine levels of binding between gp2.5 and radioactively labeled DNA. Nitrocellulose is negatively charged, so only DNA bound to gp2.5 could be retained. With increasing concentrations of gp2.5, greater amounts of single-stranded DNA were retained. The experiment only demonstrated a small amount of binding between gp2.5 and double stranded DNA. This suggests that gp2.5's molecular function is the binding of ssDNA.
|BPT3:RPOL||2016-05-01 20:37:50 CDT||GO:0003899 DNA-directed RNA polymerase activity (F)||PMID:3011596||ECO:0000314 direct assay evidence used in manual assertion|
Fig 5. The T3 gene 1.0 was over-expressed on a plasmid, and the protein product was collected. T3 mutants with no functional gene 1.0 were incapable of initiating transcription, but regained function when in the presence of collected gp1.0 protein. T7 phages without a functional copy of gene 1.0 were not affected by phage T3 gp1.0. This suggests that the T3 gene 1.0 is a T3-specific RNA polymerase.
|BPT7:RPOL||2016-05-01 20:57:10 CDT||GO:0034062 RNA polymerase activity (F)||PMID:6093820||ECO:0000314 direct assay evidence used in manual assertion|
Gene 1.0 of phage T7 was cloned into and expressed on a plasmid vector. The protein produced from the expression of gene 1.0 was demonstrated to be a T7 RNA polymerase due to its ability to transcribe RNA from T7 DNA, when in the presence of rifampicin (T7 RNA polymerase is known to be unaffected by rifampicin, which is an antibiotic that inhibits bacterial RNA polymerase).
Annotations challenged by RajivRangan
|Status||Author,Group||Page||GO Term (Aspect)||Reference||Evidence||Links||Page history|
0 annotations fixed by RajivRangan