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J. Biol. Chem., Vol. 280, Issue 5, 3251-3258, February 4, 2005
The Neisseria meningitidis Outer Membrane Lipoprotein FrpD Binds the RTX Protein FrpC*![]() From the Institute of Microbiology of the Academy of Sciences of the Czech Republic, Videnska 1083, CZ-142 20 Prague 4, Czech Republic
At conditions of low iron availability, Neisseria meningitidis produces a family of FrpC-like, type I-secreted RTX proteins of unknown role in meningococcal lifestyle. It is shown here that iron starvation also induces production of FrpD, the other protein expressed from a gene located immediately upstream of the frpC gene in a predicted iron-regulated frpDC operon. We found that FrpD is highly conserved in a set of meningococcal strains representative of all serogroups and does not exhibit any similarity to known sequences of other organisms. Subcellular localization and [3H]palmitic acid labeling in Escherichia coli revealed that FrpD is synthesized with a type II signal peptide for export across the cytoplasmic membrane and is, upon processing to a lipoprotein, sorted to the outer bacterial membrane. Furthermore, the biological function of FrpD appears to be linked to that of the RTX protein FrpC, because FrpD was found to bind the amino-proximal portion of FrpC (first 300 residues) with very high affinity (apparent Kd
Received for publication, September 30, 2004 , and in revised form, November 2, 2004. * This work was supported by Grant 310/02/1448 of the Grant Agency of the Czech Republic and by Howard Hughes Medical Institute International Research Scholarship Award 55000334 (to P. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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