The Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15525636
DOI
10.1074/jbc.m411232200
PII: S0021-9258(20)76187-9
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins chemistry genetics metabolism MeSH
- Conserved Sequence MeSH
- Lipoproteins genetics metabolism MeSH
- Membrane Proteins chemistry genetics metabolism MeSH
- Molecular Sequence Data MeSH
- Neisseria meningitidis genetics metabolism MeSH
- Bacterial Outer Membrane Proteins genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Protein Structure, Tertiary MeSH
- Calcium pharmacology MeSH
- Protein Binding MeSH
- Iron metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- frpC protein, Neisseria meningitidis MeSH Browser
- Lipoproteins MeSH
- Membrane Proteins MeSH
- Bacterial Outer Membrane Proteins MeSH
- Calcium MeSH
- Iron MeSH
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 approximately 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.
References provided by Crossref.org
Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins
Characterization of the S100A1 protein binding site on TRPC6 C-terminus
Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding
Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel
General and molecular microbiology and microbial genetics in the IM CAS
RTX proteins: a highly diverse family secreted by a common mechanism
