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Escherichia coli molybdoenzymes can be activated by protein FA from several gram-negative bacteria
C L Santini1, D Karibian, A Vasishta
1Laboratoire de Structure et fonction des Biomembranes, Département de Biologie, Faculté de Sciences de Luminy, Marseille, France.
Abstract:
Six Gram-negative bacteria (Klebsiella pneumoniae, Erwinia chrysanthemi, Proteus vulgaris, Serratia marescens, Salmonella typhimurium, and Pseudomonas aeruginosa) were shown to contain an FA-type protein capable of activating aponitrate reductase, apotrimethylamine N-oxide reductase and apoformate dehydrogenase of Escherichia coli. Protein FA activity was highest in Erwinia chrysanthemi and lowest in Pseudomonas aeruginosa. All the species also contained the low-Mr (less than or equal to 1500) heat-resistant material previously reported to be necessary for the protein-FA-dependent activation of E. coli chlB nitrate reductase.
Insights
Six Gram-negative bacteria possess an FA-type protein that activates key enzymes in Escherichia coli. This protein
Area of Science:
- Microbiology
- Enzymology
- Bacterial Metabolism
Background:
- Certain Gram-negative bacteria contain proteins that activate enzymes in other bacteria.
- Enzyme activation is crucial for metabolic pathways like nitrate reduction and dehydrogenation.
Purpose of the Study:
- To investigate the presence and activity of FA-type proteins in various Gram-negative bacteria.
- To determine the role of these proteins in activating specific bacterial enzymes.
Main Methods:
- Enzyme assays were performed on extracts from six Gram-negative bacterial species.
- Activity of FA-type protein was measured by its ability to activate aponitrate reductase, apotrimethylamine N-oxide reductase, and apoformate dehydrogenase from E. coli.
- Heat-resistant cofactor material was also assessed.
Main Results:
- An FA-type protein capable of activating E. coli enzymes was identified in Klebsiella pneumoniae, Erwinia chrysanthemi, Proteus vulgaris, Serratia marescens, Salmonella typhimurium, and Pseudomonas aeruginosa.
- Erwinia chrysanthemi exhibited the highest FA-type protein activity, while Pseudomonas aeruginosa showed the lowest.
- All tested species contained the necessary low-molecular-weight, heat-resistant cofactor for enzyme activation.
Conclusions:
- Gram-negative bacteria possess a conserved FA-type protein involved in enzyme activation.
- This protein and its associated cofactor play a significant role in bacterial metabolic processes.
- Further research can explore the specific mechanisms and broader implications of this activation system.