4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

Gibson, Jane; Dispensa, Marilyn; Fogg, George; Evans, D T; Harwood, Caroline S.

doi:10.1128/jb.176.3.634-641.1994

Cited by 77 publications

(80 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It is possible that different amino acid variations in other CoA ligases contribute to the ability of other R. palustris strains to grow with 3-CBA. The sequenced strain encodes 41 acyl-CoA ligases, two of which, benzoate-CoA ligase and 4-hydroxybenzoate-CoA ligase, react slowly with chlorinated benzoates (Geissler et al, 1988;Gibson et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Use of the Rhodopseudomonas palustris genome sequence to identify a single amino acid that contributes to the activity of a coenzyme A ligase with chlorinated substrates

Samanta¹,

Harwood²

2005

Molecular Microbiology

View full text Add to dashboard Cite

SummaryRhodopseudomonas palustris strain RCB100 degrades 3-chlorobenzoate (3-CBA) anaerobically. We purified from this strain a coenzyme A ligase that is active with 3-CBA and determined its N-terminal amino acid sequence to be identical to that of a cyclohexanecarboxylate-CoA ligase encoded by aliA from the R. palustris strain (CGA009) that has been sequenced. Strain CGA009 differs from strain RCB100 in that it does not use 3-CBA as a sole carbon source.

show abstract

Section: Discussionmentioning

confidence: 99%

Use of the Rhodopseudomonas palustris genome sequence to identify a single amino acid that contributes to the activity of a coenzyme A ligase with chlorinated substrates

Samanta¹,

Harwood²

2005

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

Section: Gene Clusters For Degradation Of Aromatic Acidsmentioning

confidence: 99%

“…Enzymes catalyzing this reaction have been purified from R. palustris (126) and from T. aromatica (24). The R. palustris gene encoding this enzyme, hbaA, was disrupted, and the resulting strain was unable to use 4-HBA as a carbon source, indicating that the HbaA enzyme is essential for the anaerobic degradation of this compound (126). The hba gene is flanked by the hbaEFGH genes, encoding a putative 4-HBA transport system related to the branched-chain amino acid uptake family of ABC transporters (312), and the hbaBCD genes, encoding 4-hydroxybenzoyl-CoA reductase (Fig.…”

Section: Gene Clusters For Degradation Of Aromatic Acidsmentioning

confidence: 99%

Anaerobic Catabolism of Aromatic Compounds: a Genetic and Genomic View

Carmona

Zamarro

Blázquez

et al. 2009

Microbiol Mol Biol Rev

386

381

View full text Add to dashboard Cite

SUMMARY Aromatic compounds belong to one of the most widely distributed classes of organic compounds in nature, and a significant number of xenobiotics belong to this family of compounds. Since many habitats containing large amounts of aromatic compounds are often anoxic, the anaerobic catabolism of aromatic compounds by microorganisms becomes crucial in biogeochemical cycles and in the sustainable development of the biosphere. The mineralization of aromatic compounds by facultative or obligate anaerobic bacteria can be coupled to anaerobic respiration with a variety of electron acceptors as well as to fermentation and anoxygenic photosynthesis. Since the redox potential of the electron-accepting system dictates the degradative strategy, there is wide biochemical diversity among anaerobic aromatic degraders. However, the genetic determinants of all these processes and the mechanisms involved in their regulation are much less studied. This review focuses on the recent findings that standard molecular biology approaches together with new high-throughput technologies (e.g., genome sequencing, transcriptomics, proteomics, and metagenomics) have provided regarding the genetics, regulation, ecophysiology, and evolution of anaerobic aromatic degradation pathways. These studies revealed that the anaerobic catabolism of aromatic compounds is more diverse and widespread than previously thought, and the complex metabolic and stress programs associated with the use of aromatic compounds under anaerobic conditions are starting to be unraveled. Anaerobic biotransformation processes based on unprecedented enzymes and pathways with novel metabolic capabilities, as well as the design of novel regulatory circuits and catabolic networks of great biotechnological potential in synthetic biology, are now feasible to approach.

show abstract

“…It does so by its direct interactions with molecular oxygen to regulate the metabolic transition between aerobic and anaerobic growth (23,41). In contrast, Rhodopseudomonas palustris HbaR, another Crp/Fnrtype transcriptional factor, regulates gene expression of the 4-hydroxybenzoate coenzyme A ligase involved in the initial enzymatic step of aromatic compound degradation (8,11,14). CooA, the only known heme protein of the Crp/Fnr-type regulators, functions as a CO-sensing transcriptional regulator and positively regulates the coo operon encoding enzymes for the oxidation of CO to CO 2 coupled with proton reduction in Rhodospi-rillum rubrum (17,38), highlighting the functional diversity of the Crp/Fnr-type regulators.…”

mentioning

confidence: 99%

Functional Characterization of Crp/Fnr-Type Global Transcriptional Regulators in Desulfovibrio vulgaris Hildenborough

Zhou

Chen

Zane

et al. 2012

Appl Environ Microbiol

View full text Add to dashboard Cite

Crp/Fnr-type global transcriptional regulators regulate various metabolic pathways in bacteria and typically function in response to environmental changes. However, little is known about the function of four annotated Crp/Fnr homologs (DVU0379, DVU2097, DVU2547, and DVU3111) in Desulfovibrio vulgaris Hildenborough. A systematic study using bioinformatic, transcriptomic, genetic, and physiological approaches was conducted to characterize their roles in stress responses. Similar growth phenotypes were observed for the crp/fnr deletion mutants under multiple stress conditions. Nevertheless, the idea of distinct functions of Crp/Fnr-type regulators in stress responses was supported by phylogeny, gene transcription changes, fitness changes, and physiological differences. The four D. vulgaris Crp/Fnr homologs are localized in three subfamilies (HcpR, CooA, and cc). The crp/fnr knockout mutants were well separated by transcriptional profiling using detrended correspondence analysis (DCA), and more genes significantly changed in expression in a ⌬DVU3111 mutant (JW9013) than in the other three paralogs. In fitness studies, strain JW9013 showed the lowest fitness under standard growth conditions (i.e., sulfate reduction) and the highest fitness under NaCl or chromate stress conditions; better fitness was observed for a ⌬DVU2547 mutant (JW9011) under nitrite stress conditions and a ⌬DVU2097 mutant (JW9009) under air stress conditions. A higher Cr(VI) reduction rate was observed for strain JW9013 in experiments with washed cells. These results suggested that the four Crp/Fnr-type global regulators play distinct roles in stress responses of D. vulgaris. DVU3111 is implicated in responses to NaCl and chromate stresses, DVU2547 in nitrite stress responses, and DVU2097 in air stress responses.T ranscription factors, promoter sequences, and regulatory circuit architecture are often referred as "the regulatory genome" (27, 33), and transcription factors are central to the function of regulatory networks (5). Organisms rely on regulatory networks to orchestrate the transcription of genes in response to internal or external environmental changes in order to optimize metabolism and enhance survival. Crp/Fnr regulators are global transcriptional regulators widely distributed in bacteria. The characteristic structure of Crp/Fnr is a C-terminal helix-turn-helix (HTH) motif that fits the DNA major groove and an N-terminal nucleotide binding domain (34). This class of transcriptional factors is named after the first two representatives discovered in Escherichia coli, i.e., the Crp (cyclic AMP [cAMP] receptor protein) and Fnr (fumarate and nitrate reductase regulator protein) (4, 21, 24, 27). Crp/Fnr regulators are generally classified into different subfamilies (e.g., CooA, Crp, Dnr, FixK, Fnr, HbaR, NnrR, etc.) according to phylogenetic affiliations (50). The increasing number of sequenced whole genomes has added to a growing list of Crp/Fnr family regulators identified in bacteria (9, 26); however, functions for most are not well defin...

show abstract

4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

Cited by 77 publications

References 50 publications

Use of the Rhodopseudomonas palustris genome sequence to identify a single amino acid that contributes to the activity of a coenzyme A ligase with chlorinated substrates

Use of the Rhodopseudomonas palustris genome sequence to identify a single amino acid that contributes to the activity of a coenzyme A ligase with chlorinated substrates

Anaerobic Catabolism of Aromatic Compounds: a Genetic and Genomic View

Functional Characterization of Crp/Fnr-Type Global Transcriptional Regulators in Desulfovibrio vulgaris Hildenborough

Contact Info

Product

Resources

About