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Category:MichSt14A 30

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StatusPageUserDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
acceptablePENCH:D3GE78Dakwalea, MichSt14A 302014-04-06 17:55:48 CDTGO:0047475 phenylacetate-CoA ligase activity (F)PMID:21625874ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 4b and 4c show the minimal activity due to lack of CoA substrate and without purified PhlC. However, when both substrate are present, there was a substantial increase in activity. Figure 2 shows that without PAA present, there are far fewer transcripts for PhlC since PAA and CoA are both needed in order for the protein to perform its ligase activity.

requireschangesSERMA:A1YZD7Dakwalea, MichSt14A 302014-04-06 15:54:55 CDTGO:0019836 hemolysis by symbiont of host erythrocytes (P)PMID:20003541ECO:0000315 mutant phenotype evidence used in manual assertion

ShlAB was responsible for direct contact hemolysis. PhlAB was responsible for extracellular hemolysis without contact. Figure 2 shows how mutants lacking PhlAB lost their hemolytic ability without contact. When these cells were given PhlAB, they regained their hemolytic activity without needing contact.

acceptableSERMA:HLYBDakwalea, MichSt14A 302014-04-06 15:11:38 CDTGO:0008320 protein transmembrane transporter activity (F)PMID:11100827ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 1 shows that organisms lacking ShlB had no hemolytic activity since no ShlA was secreted. Mutants with small changes to ShlB were still able to secrete active ShlA.

updatedbyinstructorLOCMI:S4W2D1Dakwalea, MichSt14A 302014-04-06 13:56:14 CDTGO:0016246 RNA interference (P)PMID:23792802ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 4d shows how Ago1 knockdown mutants caused far lower Vg expression, impairing vitellogenesis and egg production.

acceptableRICPR:Y027Dakwalea, MichSt14A 302014-04-06 12:35:51 CDTGO:0016278 lysine N-methyltransferase activity (F)PMID:24497633ECO:0000314 direct assay evidence used in manual assertion

Figure 2c shows the lysine residues with trimethylation sites of Outer membrane protein B.


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