Status | Page | User | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
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unacceptable | 9VIRU:Q9G046 | Connor.Long, Team Tiger1 | 2016-04-22 01:33:24 CDT | GO:1901217 regulation of holin activity (P) | PMID:21441511 | ECO:0000314 direct assay evidence used in manual assertion | "The one-step growth experiment (Fig. 7A) shows that Gp4 and Gp5, although nonessential for lysis, have an effect on the lysis timing since an Ms6 gp4 deletion mutant caused slightly accelerated lysis (80 min), whereas an Ms6 gp5 deletion mutant delayed lysis (170 min), which is consistent with holin function.These lysis times correspond to the latent time represented in Fig. 7A in addition to the initial 50 min of adsorption and were compared to the Ms6 wild-type phage (110 min) under the same experimental conditions. Thus, the absence of gp4 or gp5 in the infecting virion has an evident effect on the timing of lysis."
"These results suggest that mycobacteriophage Ms6 gp4 and gp5 encode holin proteins whose combined action could play the role of a holin and that expression of both proteins is necessary to effect host cell lysis at the correct and programmed timing, as described for other phages such as the A. naeslundii phage Av-1 (3) and the B. subtilis PBSX phage (15)."
"Moreover, interaction of Gp5 with Gp4 may contribute to very precise adjustment of the timing of hole formation and to keeping the infected cell productive, allowing the assembly of more virions."
Quotes taken from paper itself. Particular attention should be given to Figure 7A as it takes
| challenge |
unacceptable | 9VIRU:Q9G047 | Connor.Long, Team Tiger1 | 2016-04-22 01:29:25 CDT | GO:1901217 regulation of holin activity (P) | PMID:21441511 | ECO:0000314 direct assay evidence used in manual assertion | "The one-step growth experiment (Fig. 7A) shows that Gp4 and Gp5, although nonessential for lysis, have an effect on the lysis timing since an Ms6 gp4 deletion mutant caused slightly accelerated lysis (80 min), whereas an Ms6 gp5 deletion mutant delayed lysis (170 min), which is consistent with holin function.These lysis times correspond to the latent time represented in Fig. 7A in addition to the initial 50 min of adsorption and were compared to the Ms6 wild-type phage (110 min) under the same experimental conditions. Thus, the absence of gp4 or gp5 in the infecting virion has an evident effect on the timing of lysis."
"These results suggest that mycobacteriophage Ms6 gp4 and gp5 encode holin proteins whose combined action could play the role of a holin and that expression of both proteins is necessary to effect host cell lysis at the correct and programmed timing, as described for other phages such as the A. naeslundii phage Av-1 (3) and the B. subtilis PBSX phage (15)."
"Moreover, interaction of Gp5 with Gp4 may contribute to very precise adjustment of the timing of hole formation and to keeping the infected cell productive, allowing the assembly of more virions."
Quotes taken from paper itself. Particular attention should be given to Figure 7A as it takes
| challenge |
unacceptable | BPMD2:VG50 | Kaycee.Bartels, Team Tiger1 | 2016-04-20 22:23:32 CDT | GO:0008998 ribonucleoside-triphosphate reductase activity (F) | PMID:18248423 | ECO:0000314 direct assay evidence used in manual assertion | Figure 3 showed the characterization of ribonucleotide reductase activity of gp50. Figure 3b showed the enzyme could reduce of ATP to dATP. In the presence of various nucleotides, only dGTP stimulated reduction of ATP (Figure 3c). It was stated on the bottom of page 69 at the bottom of the left-hand column, that the enzyme was only found to reduce only triphosphate and not diphosphate.
| challenge |
acceptable | BPMD2:THYX | Kaycee.Bartels, Team Tiger1 | 2016-04-20 22:11:41 CDT | GO:0050797 thymidylate synthase (FAD) activity (F) | PMID:18248423 | ECO:0000314 direct assay evidence used in manual assertion | Figure 2 Shows the characterization of gp48 thymidylate synthase (ThyX) activity. Figure 2b shows that it is a flavoprotein because it contains bound FAD. It was also said to be detectable soon after the lytic phase of growth had commenced.
| challenge |
unacceptable | BPMD2:VG11 | Connor.Long, Team Tiger1 | 2016-04-20 19:14:28 CDT | GO:0051715 cytolysis in other organism (Figure 2:
- (A) The growth curve was recorded after initiating HolFL expression in E. coli BL21(DE3) (in the case of pET and pTrc vectors) and TOP10 cells (in the case of pBAD vector), at time 0, by adding IPTG (+IPTG) and arabinose (+ara), respectively.
* Measurement of E. coli when exposed to full-length Gp11. Host bacteria count decreased when exposed to gp11.
- (C) The growth curve of M. smegmatis expressing full-length Gp11 is recorded after induction with 0.2% acetamide at time 0.
* Host (M. smeg) bacterial count decreased with addition of inducer acetamide.
- (E) Growth kinetics was recorded 1 min for 60 min after induction at time 0, in a 96-well plate, for E. coli carrying specified vectors.
* Gp11 Plasmid standalone and gp11 plasmid combination (with gp10) cause lysis in host bacteria of both M.smeg and E. coli
Quotes found in the results section give overview of cytolysis function of gp11 in phage D29:
- "we find that the expression of D29 gp11 is sufficient to kill [via gp11 mediated lysis] E. coli or M. smeg."
- "Gp10 and Gp11 in E. coli results in enhanced killing of bacterial cells.") | PMID:26471254 | IDA: Inferred from Direct Assay | | challenge |
unacceptable | 9CAUD:Q2Z146 | Kaycee.Bartels, Team Tiger1 | 2016-04-11 03:41:53 CDT | GO:0016465 chaperonin ATPase complex (C) | PMID:22787217 | ECO:0000314 direct assay evidence used in manual assertion | Figure 7 shows ADP and ATP binding to recombinant gp146
Figure 8 B compares gp146 and gp188* with and without 3mM of ATP and shows that gp188* in the presence of gp146 and ATP is not affected.
| challenge |
acceptable | BPMD2:VG66 | Kaycee.Bartels, Team Tiger1 | 2016-04-07 02:05:05 CDT | GO:0004112 cyclic-nucleotide phosphodiesterase activity (F) | PMID:25307893 | ECO:0000314 direct assay evidence used in manual assertion | Figure 2 shows phosphoesterase activity of the gene product.
Figure 3 compares activity to mutated genes and shows that phosphoesterase activity goes down for mutated genes.
| challenge |
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