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Homologous npdGI genes in 2,4-dinitrophenol- and 4-nitrophenol-degrading Rhodococcus spp
Gesche Heiss1, Natalie Trachtmann, Yoshikatsu Abe
1Institute of Microbiology, University of Stuttgart, Allmandring 31, 70550 Stuttgart, Germany. gesche.heiss@po.uni-stuttgart.de
Applied and Environmental Microbiology
|May 7, 2003
Summary
Rhodococcus bacteria degrade nitrophenols using novel enzymes. These enzymes, NADPH-dependent F(420) reductase and hydride transferase II, are crucial for breaking down 2,4-dinitrophenol, representing new enzyme groups.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Rhodococcus (opacus) erythropolis HL PM-1 utilizes nitrophenols as nitrogen sources.
- The enzymes NADPH-dependent F(420) reductase (NDFR) and hydride transferase II (HTII) facilitate nitrophenol conversion via hydride Meisenheimer complexes.
Purpose of the Study:
- To investigate the npdG and npdI genes encoding NDFR and HTII in other 2,4-dinitrophenol (2,4-DNP) degrading Rhodococcus species.
- To confirm the role of these genes in 2,4-DNP degradation through heterologous expression.
- To analyze conserved domains and phylogenetic relationships of these enzymes.
Main Methods:
- Gene amplification of npdG and npdI from six Rhodococcus strains.
- Heterologous expression of amplified genes.
- Sequence analysis and phylogenetic analysis of NDFRs and HTIIs.
Main Results:
- Amplified npdG and npdI genes showed high sequence similarity (86-99%) to those of strain HL PM-1.
- Heterologous expression confirmed the involvement of these genes in 2,4-DNP degradation.
- Sequence analyses revealed conserved domains for NADPH or F(420) binding.
- Phylogenetic analyses identified NDFRs and HTIIs as potentially novel groups within F(420)-dependent enzyme families.
Conclusions:
- NDFR and HTII enzymes from various Rhodococcus species are involved in 2,4-DNP catabolism.
- These enzymes represent novel groups of F(420)-dependent enzymes.
- The findings contribute to understanding microbial degradation pathways of nitroaromatic compounds.
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