GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:22761913
| Citation |
Martos, A, Monterroso, B, Zorrilla, S, Reija, B, Alfonso, C, Mingorance, J, Rivas, G and Jiménez, M (2012) Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli. PLoS ONE 7:e39829 |
|---|---|
| Abstract |
We have obtained milligram amounts of highly pure Escherichia coli division protein FtsA from inclusion bodies with an optimized purification method that, by overcoming the reluctance of FtsA to be purified, surmounts a bottleneck for the analysis of the molecular basis of FtsA function. Purified FtsA is folded, mostly monomeric and interacts with lipids. The apparent affinity of FtsA binding to the inner membrane is ten-fold higher than to phospholipids, suggesting that inner membrane proteins could modulate FtsA-membrane interactions. Binding of FtsA to lipids and membranes is insensitive to ionic strength, indicating that a net contribution of hydrophobic interactions is involved in the association of FtsA to lipid/membrane structures. |
| Links |
PubMed PMC3384640 Online version:10.1371/journal.pone.0039829 |
| Keywords |
|
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0051301: cell division |
ECO:0000314: |
P |
Figure 3 shows the interactions of ftsA with lipid/membrane structures. Figure 3c specifically shows ionic strength of ftsA binding. |
complete | ||||
See also
References
See Help:References for how to manage references in GONUTS.
