Public
Assessment | Ivanerill | 2018-07-24 12:39:07 CDT | No notes given. | Acceptable
✔ Protein
✔ Publication
✔ Qualifier
✔ Go term
✔ Evidence
✔ With/From
✔ Notes
✔ Unique/Original
|
Public
Assessment | DanielRenfro | 2018-07-20 03:53:39 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0009898 |
cytoplasmic side of plasma membrane |
PMID:23024349 |
IDA: Inferred from Direct Assay |
|
C |
This study about PspC topology allows authors to propose a new working model for activation of the Psp system. Although there have been conflicting past studies on the topology of the shock protein PspC, through multiple direct assays and an in silico analysis with TOPCON, the server for membrane protein topology prediction, the study shows that both the N and C termini of the protein are located in the cytoplasm. The C terminus, which might be the recognition site for FtsH protease and an interaction interface with PspA, would function in the cytoplasm, not the periplasm. In the assay with chemical modification of cysteine residues, seen in Figure 4, CpxP is shown to be located in the periplasm and confirms that 3-maleimidylpropionyl biocytin (MPB) can cross the outer membrane, as in Figure 4A. All PspB cysteine substitution mutants were labeled by MPB only after cell disruption, agreeing with its C terminus location in the cytoplasm, as in Figure B, which is information that has been supported well before. However, all of the PspC cysteine substitution mutants were also labeled only after sonication, whether the cysteine was in the N or C terminus or not, which is shown by the image 4C. This confirms that both ends of PspC are on the cytoplasmic side of the membrane. |
complete
CACAO 13300
| on YEREN:Q9F4H2
| Flagged
|
Public
Assessment | DanielRenfro | 2018-07-18 06:26:40 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0009898 |
cytoplasmic side of plasma membrane |
PMID:23024349 |
IDA: Inferred from Direct Assay |
|
C |
This study about PspC topology allows authors to propose a new working model for activation of the Psp system. Although there have been conflicting past studies on the topology of the shock protein PspC, through multiple direct assays and an in silico analysis with TOPCON, the server for membrane protein topology prediction, the study shows that both the N and C termini of the protein are located in the cytoplasm. The C terminus, which might be the recognition site for FtsH protease and an interaction interface with PspA, would function in the cytoplasm, not the periplasm. In the assay with chemical modification of cysteine residues, seen in Figure 4, CpxP is biotinylated robustly before sonication, which agrees that it is located in the periplasm and confirms that 3-maleimidylpropionyl biocytin (MPB) can cross the Y. enterocolitica outer membrane. All PspB cysteine substitution mutants were labeled by MPB only after cell disruption, agreeing with its C terminus location in the cytoplasm. All of the PspC cysteine substitution mutants were also labeled only after sonication, whether the cysteine was in the N or C terminus or not. This confirms that both ends of PspC are on the cytoplasmic side of the membrane. |
complete
CACAO 13300
| on YEREN:Q9F4H2
| Flagged
|
Public
Assessment | Ivanerill | 2018-07-18 04:55:39 CDT | Your notes provide a lot of background and thoroughly describe Fig. 4, to the point that it is hard to see what part of Fig. 4 you are annotating. Please reword so that it becomes clear what part of Fig. 4 is essential to your annotation, and how the figure supports your claim.
Note also that there are more specific GO terms that you could use to describe the localization of PspC based on Fig. 4 results.
| Requires Changes
✔ Protein
✔ Publication
✔ Qualifier
✗ Go term
✗ Evidence
✔ With/From
✗ Notes
✔ Unique/Original
|
