Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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de Brouwer, A.P. et al.

de Brouwer, Bouma, van Tiel, Heerma, Brouwers, Bevers, Westerman, Roelofsen, Wirtz,

The binding of phosphatidylcholine to the phosphatidylcholine transfer protein: affinity and role in folding.

Bovine liver phosphatidylcholine transfer protein (PC-TP) has been expressed in Escherichia coli and purified to homogeneity from the cytosol fraction at a yield of 0.45 mg PC-TP per 10 mg total cytosolic protein. In addition, active PC-TP was obtained from inclusion bodies. An essential factor in the activation of PC-TP was phosphatidylcholine (PC) present in the folding buffer. PC-TP from the cytosol contains phosphatidylethanolamine (PE) and phosphatidylglycerol (PG) with a preference for the di-monounsaturated species over the saturated species as determined by fast atom bombardment mass spectrometry (FAB-MS). By incubation with microsomal membranes the endogenous PE and PG were replaced by PC. Relative to the microsomal PC species composition, PC-TP bound preferentially C16:0/C20:4-PC and C16:0/C18:2-PC (twofold enriched) whereas the major microsomal species C18:0/C18:1-PC and C18:0/C18:2-PC were distinctly less bound. PC-TP is structurally homologous to the lipid- binding domain of the steroidogenic acute regulatory protein (Nat. Struct. Biol. 7 (2000) 408). Replacement of Lys(55) present in one of the beta-strands forming the lipid-binding site, with an isoleucine residue yielded an inactive protein. This suggests that Lys(55) be involved in the binding of the PC molecule.[1]

References

The binding of phosphatidylcholine to the phosphatidylcholine transfer protein: affinity and role in folding. de Brouwer, A.P., Bouma, B., van Tiel, C.M., Heerma, W., Brouwers, J.F., Bevers, L.E., Westerman, J., Roelofsen, B., Wirtz, K.W. Chem. Phys. Lipids (2001) [Pubmed]

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