The Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC

doi:10.1074/jbc.M411232200

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on February 4, 2005

This Article

	Full Text (Accepted Manuscript)
	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

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?

Papers In Press, published online ahead of print November 2, 2004
J. Biol. Chem, 10.1074/jbc.M411232200
Submitted on September 30, 2004
Revised on November 2, 2004
Accepted on November 2, 2004

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

Laboratory of Molecular Biology of Bacterial Pathogens, Institute of Microbiology, Czech Academy of Sciences, Prague 142 20

Corresponding Author: sebo{at}biomed.cas.cz

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 starvation for iron induces also 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 E. 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, since FrpD was found to bind the amino-proximal portion of FrpC (first 300 residues) with very high affinity (apparent Kd ~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.

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati 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]

All ASBMB Journals	Molecular and Cellular Proteomics
Journal of Lipid Research	ASBMB Today

				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]