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

0022207 - MBÚ 2006 RIV SIGLE US eng J - Journal Article
Procházková, Kateřina - Osička, Radim - Linhartová, Irena - Halada, Petr - Šulc, Miroslav - Šebo, Peter
The Neisseria meningitidis Outer Membrane Lipoprotein FrpD Binds the RTX Protein FrpC.
[Lipoprotein FrpD z vnější membrány Neisseria meningitidis váže RTXC protein FrpD.]
Journal of Biological Chemistry. Roč. 280, č. 5 (2005), s. 3251-3258. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GA310/02/1448
Grant - others:Howard Hughes Medical Institute International Research Scholarship Award 55000334
Institutional research plan: CEZ:AV0Z50200510
Keywords : neisseria meningitidis * FrpD * FrpC
Subject RIV: EE - Microbiology, Virology
Impact factor: 5.854, year: 2005

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.

V podmínkách limitace růstu meningokoků koncentrací volného železa exprimují tyto protein FrpD. V práci je ukázáno, že se jedná o lipoprotein, který je lokalizovánm do vnější bakteriální membrány a váže sekretovaný RTX protein FrpC z vysokou afinitou
Permanent Link: http://hdl.handle.net/11104/0110990