Analysis in Neisseria meningitidis and other Neisseria species of genes homologous to the FKBP immunophilin family
- 27 October 1993
- journal article
- Published by Wiley in Molecular Microbiology
- Vol. 10 (1) , 13-23
- https://doi.org/10.1111/j.1365-2958.1993.tb00899.x
Abstract
The immunophilin family of FK506-binding proteins (FKBPs), involved in eukaryotic protein-folding and cell regulation, have recently been found to have prokaryotic homologues. Genes with sequences homologous to those encoding human FKBPs were examined in Neisseria species. An FKBP DNA sequence was present, as shown by the polymerase chain reaction and Southern blotting experiments, in the chromosome of Neisseria meningitidis (14 strains) and in all 11 different commensal Neisseria spp. studied, but was not found in Neisseria gonorrhoeae (11 strains tested) or in Moraxella catarrhalis. The nucleotide and predicted protein sequences of the FKBP-encoding domain from five of the meningococcal strains were highly conserved (e.g. > or = 97% homologous). The meningococcal nucleotide sequence was > or = 93% homologous and the consensus meningococcal protein sequence was > or = 97% homologous to FKBP sequences found in seven different commensal Neisseria spp. The meningococcal nucleotide and predicted protein sequences were > or = 59% homologous to the conserved C-terminus of the human FKBP gene family. The FKBP nucleotide sequence was present as a single copy in the chromosome of commensal Neisseria spp. and in most strains of N. meningitidis. The FKBP gene was linked to the silent pilin locus, pilS, in class II-piliated meningococcal strains. In meningococcal strains expressing class I pili, the FKBP gene was linked to one of several pilS loci but not the pilE locus present in these strains. FKBP genes found in commensal Neisseria spp. were not linked to known pilin loci.Keywords
This publication has 50 references indexed in Scilit:
- Leukocyte chemotactic activity of FKBP and inhibition by FK506Biochemical and Biophysical Research Communications, 1992
- Mip protein of Legionella pneumophila exhibits peptidyl‐prolyl‐cis/trans isomerase (PPIase) activityMolecular Microbiology, 1992
- Basic fibroblast growth factor induces 3T3 fibroblasts to synthesize and secrete a cyclophilin-like protein and β2-microglobulinBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1991
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexesCell, 1991
- Binding by designNature, 1991
- FK506 and protein kinase CNature, 1991
- Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cellsBiochemistry, 1991
- Rapamycin and FK506 binding proteins (immunophilins)Journal of the American Chemical Society, 1991
- Chemistry and Biology of the Immunophilins and Their Immunosuppressive LigandsScience, 1991
- Nucleotide sequence of a regulatory region controlling alginate synthesis in Pseudomonas aeruginosa: characterization of the algR2 geneGene, 1989