Roosendaal E, Jacobs A A, Rathman P, Sondermeyer C, Stegehuis F, Oudega B, de Graaf F K
Department of Molecular Microbiology, Vrije Universiteit, Amsterdam, The Netherlands.
Mol Microbiol. 1987 Sep;1(2):211-7. doi: 10.1111/j.1365-2958.1987.tb00514.x.
Analysis of the nucleotide sequence of the distal part of the fan gene cluster encoding the proteins involved in the biosynthesis of the fibrillar adhesin, K99, revealed the presence of two structural genes, fanG and fanH. The amino acid sequence of the gene products (FanG and FanH) showed significant homology to the amino acid sequence of the fibrillar subunit protein (FanC). Introduction of a site-specific frameshift mutation in fanG or fanH resulted in a simultaneous decrease in fibrillae production and adhesive capacity. Analysis of subcellular fractions showed that, in contrast to the K99 fibrillar subunit (FanC), both the FanH and the FanG protein were loosely associated with the outer membrane, possibly on the periplasmic side, but were not components of the fimbriae themselves.
