HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 5, 3251-3258, February 4, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/5/3251    most recent M411232200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Prochazkova, K. Articles by Sebo, P. Search for Related Content PubMed PubMed Citation Articles by Prochazkova, K. Articles by Sebo, P. Social Bookmarking                      What's this?

The Neisseria meningitidis Outer Membrane Lipoprotein FrpD Binds the RTX Protein FrpC^*

Katerina Prochazkova, Radim Osicka, Irena Linhartova, Petr Halada, Miroslav Sulc, and Peter Sebo

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 K_d 0.2 nM). These results suggest that FrpD represents an rtx loci-encoded accessory lipoprotein that could be involved in anchoring of the secreted RTX protein to the outer bacterial membrane.

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.

To whom correspondence should be addressed: Inst. of Microbiology Czech Academy of Sciences, Vídenska 1083, CZ-142 20 Prague 4, Czech Republic. Tel.: 420-241-062-762; Fax: 420-241-062-152; E-mail: sebo{at}biomed.cas.cz.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Elias and U. Vogel IS1301 Fingerprint Analysis of Neisseria meningitidis Strains Belonging to the ET-15 Clone J. Clin. Microbiol., January 1, 2007; 45(1): 159 - 167. [Abstract] [Full Text] [PDF]

				D. Parker, R. M. Kennan, G. S. Myers, I. T. Paulsen, J. G. Songer, and J. I. Rood Regulation of Type IV Fimbrial Biogenesis in Dichelobacter nodosus J. Bacteriol., July 1, 2006; 188(13): 4801 - 4811. [Abstract] [Full Text] [PDF]

				K. G. Wooldridge, M. Kizil, D. B. Wells, and D. A. A. Ala'Aldeen Unusual Genetic Organization of a Functional Type I Protein Secretion System in Neisseria meningitidis Infect. Immun., September 1, 2005; 73(9): 5554 - 5567. [Abstract] [Full Text] [PDF]