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The Pseudomonas aeruginosa pilK gene encodes a chemotactic methyltransferase (CheR) homologue that is translationally regulated
Author(s) -
Darzins Aldis
Publication year - 1995
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.1365-2958.1995.tb02379.x
Subject(s) - biology , mutant , complementation , lac operon , gene , open reading frame , genetics , bacillus subtilis , operon , escherichia coli , protein fragment complementation assay , myxococcus xanthus , peptide sequence , microbiology and biotechnology , bacteria
Summary A new locus, designated pilK , located immediately adjacent to the previously described Pseudomonas aeruginosa pilG–J gene cluster, has been identified. Sequence analysis of a 1.3 kb region revealed the presence of a single open reading frame of 291 amino acid residues (M r , 33 338) that contained significant homology to the chemotactic methyltransferase proteins of Escherichia coli. Bacillus subtilis and the gliding bacterium Myxococcus xanthus. The 60 bp pilJ–pilK intergenic region was devoid of promoter consensus sequences, suggesting that pilj and pilK are contained within the same transcriptional unit. The intergenic region did contain, however, a large, highly GC‐rich, inverted repeat that prevented PilK production in expression studies. To investigate the regulatory role of these sequences, pilK‐lacZ gene fusions, as well as derivatives containing sequence alterations in the potential stem‐loop region, were constructed and analysed in E. coli and P. aeruginosa. Modification of the inverted repeat region in pilK‐lacZ protein fusion constructs resulted in as much as a 24'fold increase in β‐galactosidase activity, whereas similar modifications in pilK‐lacZ transcriptional fusions had only a marginal effect on β‐galactosidase levels. These results indicated that PilK production may be largely regulated at the level of translation. In stark contrast to pilG‐J mutants, which are dramatically impaired in pilus production and/or function, a PAO1 pilK deletion mutant was indistinguishable from the wild type. In addition, complementation studies suggested that the PilK and E. coli CheR proteins are not functionally interchangeable.

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