PMID:16364305
| Citation |
Ahuja, U and Thöny-Meyer, L (2006) The membrane anchors of the heme chaperone CcmE and the periplasmic thioredoxin CcmG are functionally important. FEBS Lett. 580:216-22 |
|---|---|
| Abstract |
The cytochrome c maturation system of Escherichia coli contains two monotopic membrane proteins with periplasmic, functional domains, the heme chaperone CcmE and the thioredoxin CcmG. We show in a domain swap experiment that the membrane anchors of these proteins can be exchanged without drastic loss of function in cytochrome c maturation. By contrast, the soluble periplasmic forms produced with a cleavable OmpA signal sequence have low biological activity. Both the chimerical CcmE (CcmG'-'E) and the soluble periplasmic CcmE produce low levels of holo-CcmE and thus are impaired in their heme receiving capacity. Also, both forms of CcmE can be co-precipitated with CcmC, thus restricting the site of interaction of CcmE with CcmC to the C-terminal periplasmic domain. However, the low level of holo-CcmE formed in the chimera is transferred efficiently to cytochrome c, indicating that heme delivery from CcmE does not involve the membrane anchor. |
| Links |
PubMed Online version:10.1016/j.febslet.2005.12.006 |
| Keywords |
Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Biological Transport/genetics; Cytochromes c/genetics; Cytochromes c/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heme/genetics; Heme/metabolism; Hemeproteins/genetics; Hemeproteins/metabolism; Periplasm/enzymology; Periplasm/genetics; Protein Disulfide Reductase (Glutathione)/genetics; Protein Disulfide Reductase (Glutathione)/metabolism; Protein Processing, Post-Translational/physiology; Protein Structure, Tertiary/genetics; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Thioredoxins/genetics; Thioredoxins/metabolism |
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