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H-NOX Influences Biofilm Formation, Central Metabolism, and Quorum Sensing in Paracoccus denitrificans .
- Source :
-
Journal of proteome research [J Proteome Res] 2024 Nov 01; Vol. 23 (11), pp. 4988-5000. Date of Electronic Publication: 2024 Oct 06. - Publication Year :
- 2024
-
Abstract
- The transition from planktonic to biofilm growth in bacteria is often accompanied by greater resistance to antibiotics and other stressors, as well as distinct alterations in physical traits, genetic activity, and metabolic restructuring. In many species, the heme nitric oxide/oxygen binding proteins (H-NOX) play an important role in this process, although the signaling mechanisms and pathways in which they participate are quite diverse and largely unknown. In Paracoccus denitrificans , deletion of the hnox gene results in a severe biofilm-deficient phenotype. Quantitative proteomics was used to assemble a comprehensive data set of P. denitrificans proteins showing altered abundance of those involved in several important metabolic pathways. Further, decreased levels of pyruvate and elevated levels of C <subscript>16</subscript> homoserine lactone were detected for the Δhnox strain, associating the biofilm deficiency with altered central carbon metabolism and quorum sensing, respectively. These results expand our knowledge of the important role of H-NOX signaling in biofilm formation.
- Subjects :
- Proteomics methods
4-Butyrolactone analogs & derivatives
4-Butyrolactone metabolism
Pyruvic Acid metabolism
Signal Transduction
Heme-Binding Proteins metabolism
Metabolic Networks and Pathways genetics
Gene Expression Regulation, Bacterial
Hemeproteins metabolism
Hemeproteins genetics
Biofilms growth & development
Paracoccus denitrificans metabolism
Paracoccus denitrificans genetics
Quorum Sensing
Bacterial Proteins metabolism
Bacterial Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1535-3907
- Volume :
- 23
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Journal of proteome research
- Publication Type :
- Academic Journal
- Accession number :
- 39370609
- Full Text :
- https://doi.org/10.1021/acs.jproteome.4c00466