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The Neisseria meningitidis Outer Membrane Lipoprotein FrpD Binds the RTX Protein FrpC
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SYSNO ASEP 0022207 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title The Neisseria meningitidis Outer Membrane Lipoprotein FrpD Binds the RTX Protein FrpC Title Lipoprotein FrpD z vnější membrány Neisseria meningitidis váže RTXC protein FrpD Author(s) Procházková, Kateřina (MBU-M)
Osička, Radim (MBU-M) RID, ORCID
Linhartová, Irena (MBU-M) RID, ORCID
Halada, Petr (MBU-M) RID, ORCID
Šulc, Miroslav (MBU-M) RID, ORCID
Šebo, Peter (MBU-M) RID, ORCIDSource Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 280, č. 5 (2005), s. 3251-3258Number of pages 8 s. Language eng - English Country US - United States Keywords neisseria meningitidis ; FrpD ; FrpC Subject RIV EE - Microbiology, Virology R&D Projects GA310/02/1448 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50200510 - MBU-M (2005-2011) Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2006
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