ABCC8 p.Arg193Gln
| Predicted by SNAP2: | A: N (53%), C: N (53%), D: D (85%), E: D (66%), F: D (63%), G: D (71%), H: N (57%), I: D (63%), K: N (82%), L: N (66%), M: D (66%), N: N (66%), P: D (75%), Q: N (61%), S: N (61%), T: N (66%), V: D (59%), W: D (80%), Y: D (66%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: N, F: D, G: D, H: N, I: D, K: N, L: D, M: D, N: N, P: D, Q: N, S: D, T: D, V: D, W: D, Y: D, |
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[hide] ZipN, an FtsA-like orchestrator of divisome assemb... Mol Microbiol. 2009 Oct;74(2):409-20. Epub 2009 Sep 8. Marbouty M, Saguez C, Cassier-Chauvat C, Chauvat F
ZipN, an FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803.
Mol Microbiol. 2009 Oct;74(2):409-20. Epub 2009 Sep 8., [PMID:19737354]
Abstract [show]
We pursued the characterization of the divisome of the spherical-celled cyanobacterium Synechocystis PCC6803, through deletion, site-directed mutagenesis, GFP tagging, two-hybrid and co-immunoprecipitation assays. We presently report that the DivIVA-like protein Cdv3 is essential to both cell growth and division, whereas the AmiC, AmpH, FtsE, FtsN, SpoIID, YlmD, YlmE and YlmG proteins are dispensable. With the exception of the self-interacting protein YlmD, none of these dispensable factors appeared to interact with ZipN, the crucial cytokinetic factor we previously characterized. By contrast, we found that ZipN interacts with itself and the self-interacting protein Cdv3, as well as with all other crucial cytokinetic factors we previously characterized, namely: FtsZ, FtsI, FtsQ, SepF and ZipS. We also identified ZipN amino acids selectively involved in ZipN interaction with one of its following partners, Cdv3, FtsQ or SepF. Finally, we found no direct interaction between Cdv3, SepF and ZipS. Collectively, these results indicate that ZipN is a central player of divisome assembly in cyanobacteria, similarly to the FtsA protein of E. coli that is absent in cyanobacteria and chloroplast.
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No. Sentence Comment
58 For instance, the mutation R190Q abolished the ZipN/SepF interaction (like the double mutation R147Q/E148Q); the two mutations R193Q and D307N prevented the ZipN/Cdv3 interaction; and the mutation R208Q impaired the ZipN/ FtsQ interaction.
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ABCC8 p.Arg193Gln 19737354:58:127
status: NEW130 These selective mutations are the two mutations R190Q and R147Q/E148Q that each abolished ZipN/SepF interaction; the two mutations R193Q and D307N that each prevents the ZipN/Cdv3 interaction; and R208Q that impaired the ZipN/FtsQ interaction (Fig. 2).
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ABCC8 p.Arg193Gln 19737354:130:131
status: NEW