- PII
- 10.31857/S0026365624040062-1
- DOI
- 10.31857/S0026365624040062
- Publication type
- Status
- Published
- Authors
- Volume/ Edition
- Volume 93 / Issue number 4
- Pages
- 438-443
- Abstract
- Phosphonates are alternative phosphorus sources for bacteria. The genome of Achromobacter insolitus strain LCu2 contains three predicted phn clusters of ABC-type phosphonate transporters into the cell. To understand the functional, evolutionary, and ecological role of the phn clusters, phylogenetic analysis of substrate-binding PhnD proteins from strain LCu2 with their homologs in other Achromobacter species and in closely related genera of the family Alcaligenaceae was carried out. The PhnD transporters formed three separate clusters, which indicated the differences in their structural composition. PhnD1 and PhnD2 were present in the genomes of all Achromobacter species and grouped separately from those of other members of the family Alcaligenaceae, which indicated vertical inheritance of the phnD1 and phnD2 genes and their involvement in the life-supporting processes. PhnD3 was found in the genomes of seven Achromobacter species. The phnD3 gene was probably acquired via horizontal transfer or duplication and is induced during adaptation to changing environmental conditions. Maintenance of three structurally different clusters of the phn transporters is probably ecologically advantageous to A. insolitus LCu2, providing for phosphorus retrieval from synthetic and natural organophosphonates as well as other sources.
- Keywords
- фосфонаты phn транспортеры Achromobacter insolitus филогения Alcaligenaceae
- Date of publication
- 15.07.2024
- Year of publication
- 2024
- Number of purchasers
- 0
- Views
- 31
References
- 1. Amstrup S. K., Ong S. C., Sofos N., Karlsen J. L., Skjerning R. B., Boesen T., Enghold J. J., Hove-Jensen B., Brodersen D. E. Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase // Nat. Commun. 2023. V. 14. Art. 1001. https://doi.org/10.1038/s41467-023-36604-y
- 2. Hove-Jensen B., Zechel D. L., Jochimsen B. Utilization of glyphosate as phosphate source: biochemistry and genetics of bacterial carbon-phosphorus lyase // Microbiol. Mol. Biol. Rev. 2014. V. 78. P. 176‒197.
- 3. Kertesz M., Elgorriaga A., Amrhein N. Evidence for two distinct phosphonate-degrading enzymes (C‒P lyases) in Arthrobacter sp. GLP-1 // Biodegradation. 1991. V. 2. P. 53‒59.
- 4. Krol E., Becker A. Global transcriptional analysis of the phosphate starvation response in Sinorhizobium meliloti strains 1021 and 2011 // Mol. Genet. Genom. 2004. V. 272. P. 1‒17.
- 5. Kumar S., Stecher G., Li M., Knyaz C., Tamura K. MEGA X: Molecular Evolutionary Genetics Analysis across computing platforms // Mol. Biol. Evol. 2018. V. 35. P. 1547‒1549.
- 6. Shah B. S., Ford B. A., Varkey D., Mikolajek H., Orr C., Mykhaylyk V., Owens R. J., Paulsen I. T. Marine picocyanobacterial PhnD1 shows specificity for various phosphorus sources but likely represents a constitutive inorganic phosphate transporter // ISME J. 2023. V. 17. P. 1040‒1051.
- 7. Sievers F., Wilm A., Dineen D., Gibson T. J., Karplus K., Li W., Lopez R., McWilliam H., Remmert M., Söding J., Thompson J. D., Higgins D. G. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega // Mol. Syst. Biol. 2011. V. 7. Art. 539.
- 8. Zavaleta-Pastor M., Sohlenkamp C., Gao J. L., Guan Z., Zaheer R., Finan T. M., Geiger O. Sinorhizobium meliloti phospholipase C required for lipid remodeling during phosphorus limitation // Proc. Natl. Acad. Sci. USA. 2010. V. 107. P. 302‒307.