We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A histidine decarboxylase gene encoded by the Vibrio anguillarum plasmid pJM1 is essential for virulence: histamine is a precursor in the biosynthesis.
- Authors
Tolmasky, Marcelo E.; Actis, Luis A.; Crosa, Jorge H.
- Abstract
We have identified and sequenced an <em>hdc</em> gene in the <em>Vibrio anguillarum</em> plasmid pJMI which encodes a histldine decarboxyiase enzyme and is an essential component for the biosynthesis of anguibactin. The open reading frame corresponds to a protein of 386 amino acids with a calculated molecular mass of 44 259.69 Da. The amino acid sequence has extensive homology with the pyridoxal-P-dependent histidine decarboxylases of <em>Morganella morganii, Klebsiella planticola</em>, and <em>Enterobacter aerogenes</em>. Tn<em>3</em>-HoHo1 transposition mutagenesis of the <em>hdc</em> gene present in a recombinant clone carrying the entire pJMI Iron uptake region produced two derivatives, one with the <em>lacZ</em> gene in the same orientation as the direction of <em>hdc</em> transcription and the other with the <em>lacZ</em> gene in the opposite orientation. A <em>V. anguillarum</em> strain harbouring one of the mutated derivatives was unable to grow under iron-limiting conditions and did not produce anguibactin. Therefore, the <em>hdc</em> gene must play a role in the biosynthetic pathway of this siderophore and consequently in conferring the high virulence phenotype to this bacterium. The role of histidine decarboxylase in biosynthesis of anguibactin was confirmed by the fact that growth under iron starvation was restored by addition of histamine to the medium. The presence of anguibactin was also demonstrated in supernatants from cultures of the <em>hdc</em> mutant strains grown under iron starvation with the addition of histamine, further confirming that histamine is a precursor in the biosynthesis of the...
- Subjects
GENES; VIBRIO; SPIRILLACEAE; PLASMIDS; DECARBOXYLASES; ENZYMES
- Publication
Molecular Microbiology, 1995, Vol 15, Issue 1, p87
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.1995.tb02223.x