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Primary structure and subcellular localization of two fimbrial subunit‐like proteins involved in the biosynthesis of K99 fibrillae
Author(s) -
Roosendaal E.,
Jacobs A. A. C.,
Rathman P.,
Sondermeyer C.,
Stegehuis F.,
Oudega B.,
Graaf F. K.
Publication year - 1987
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1987.tb00514.x
Subject(s) - biology , periplasmic space , protein subunit , gene , peptide sequence , biochemistry , gene cluster , homology (biology) , structural gene , protein primary structure , fimbria , amino acid , biosynthesis , genetics , escherichia coli
Summary 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 frame‐shift mutation in lanG 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.