Applied and Environmental Microbiology, December 2001, p. 5801-5809, Vol. 67, No. 12
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.12.5801-5809.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Departments of Marine Sciences1 and Microbiology,2 University of Georgia, Athens, Georgia 30602
Received 27 June 2001/Accepted 26 September 2001
Degradation of lignin-related aromatic compounds is an important
ecological process in the highly productive salt marshes of the
southeastern United States, yet little is known about the mediating
organisms or their catabolic pathways. Here we report the diversity of
a gene encoding a key ring-cleaving enzyme of the
-ketoadipate
pathway, pcaH, amplified from bacterial communities associated with decaying Spartina alterniflora, the salt
marsh grass that dominates these coastal systems, as well as from
enrichment cultures with aromatic substrates
(p-hydroxybenzoate, anthranilate, vanillate, and
dehydroabietate). Sequence analysis of 149 pcaH clones
revealed 85 unique sequences. Thirteen of the 53 amino acid residues
compared were invariant in the PcaH proteins, suggesting that these
residues have a required catalytic or structural function. Fifty-eight
percent of the clones matched sequences amplified from a collection of
36 bacterial isolates obtained from seawater, marine sediments, or
senescent Spartina. Fifty-two percent of the
pcaH clones could be assigned to the roseobacter group, a marine lineage of the class
-Proteobacteria abundant in
coastal ecosystems. Another 6% of the clones matched genes retrieved
from isolates belonging to the genera Acinetobacter,
Bacillus, and Stappia, and 42% of the clones could
not be assigned to a cultured bacterium based on sequence identity.
These results suggest that the diversity of the genes encoding a single
step in aromatic compound degradation in the coastal marsh examined is high.
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