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SadB, a mediator of AmrZ proteolysis and biofilm development in Pseudomonas aeruginosa
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“Loss of sadB locks cells into a surface-defective, hyperswarming state and identifies sadB as a gatekeeper that also acts as a posttranslational modulator of AmrZ [25,26,27].”
From Understanding Pseudomonas aeruginosa Biofilms: Quorum Sensing, c-di-GMP Signaling, and Emerging Antibiofilm Approaches (2026) · cites this paper as [26]
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Structural history of human SRGAP2 proteins
Sporny, M., Guez-Haddad, J., Kreusch, A., Shakartzi, S., Neznansky, A., Cross, A., Isupov, M. N., Qualmann, B., Kessels, M. M., & Opatowsky, Y. (2017) · Molecular Biology and Evolution · doi:10.1093/molbev/msx094 · Cited by 41
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Research works printed but not linked: 55
- Hsueh, P. R. et al. Persistence of a multidrug-resistant Pseudomonas aeruginosa clone in an intensive care burn unit. J. Clin. Microbiol 36, 1347–1351 (1998). · doi:10.1128/jcm.36.5.1347-1351.1998
- Aloush, V., Navon-venezia, S., Seigman-igra, Y., Cabili, S. & Carmeli, Y. Multidrug-resistant Pseudomonas aeruginosa: risk factors and clinical impact. Society 50, 43–48 (2006).
- Kwon, S., Schweizer, M. L. & Perencevich, E. N. National Institute of Allergy and Infectious Disease (NIAID) funding for studies of hospital-associated bacterial pathogens: are funds proportionate to burden of disease?. Antimicrob. Resist Infect. Control 1, 5 (2012). · doi:10.1186/2047-2994-1-5
- Hirsch, E. B. & Tam, V. H. Impact of multidrug-resistant Pseudomonas aeruginosa infection on patient outcomes. Expert Rev. Pharmacoecon Outcomes Res. 10, 1–18 (2011).
- Hill, D. et al. Antibiotic susceptibility of Pseudomonas aeruginosa isolates derived from patients with cystic fibrosis under aerobic, anaerobic, and biofilm conditions. J. Clin. Microbiol 43, 5085–5090 (2005). · DOI · Paper page
- Bjarnsholt, T. The role of bacterial biofilms in chronic infections. APMIS Suppl. https://doi.org/10.1111/apm.12099. (2013). · DOI · Paper page
- Moreau-Marquis, S., Stanton, B. & O’Toole, G. Pseudomonas aeruginosa biofilm formation in the cystic fibrosis airway. Pulm. Pharmacol. Ther. 21, 595–599 (2008). · DOI · Paper page
- Wozniak, D. J. & Mann, E. E. Pseudomonas biofilm matrix composition and niche biology. FEMS. Microbiol. Rev. 33, 395–401 (2015).
- Mikkelsen, H., Sivaneson, M. & Filloux, A. Key two-component regulatory systems that control biofilm formation in Pseudomonas aeruginosa. Environ. Microbiol. 13, 1666–1681 (2011). · DOI · Paper page
- Schurr, M. J. Which bacterial biofilm exopolysaccharide is preferred, psl or alginate?. J. Bacteriol. 195, 1623–1626 (2013). · doi:10.1128/jb.00173-13
- Valentini, M. & Filloux, A. Biofilms and cyclic di-GMP (c-di-GMP) signaling: lessons from Pseudomonas aeruginosa and other bacteria. J. Biol. Chem. 291, 12547–12555 (2016). · DOI · Paper page
- Merritt, J. udithH. et al. Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases. mBio 1, 1–9 (2010). · DOI · Paper page
- Petrova, O. E., Cherny, K. E. & Sauer, K. The Pseudomonas aeruginosa diguanylate cyclase GcbA, a homolog of P. Fluorescens GcbA, promotes initial attachment to surfaces, but not biofilm formation, via regulation of motility. J. Bacteriol. 196, 2827–2841 (2014). · DOI
- Ha, D.-G. & O’Toole, G. A. c-di-GMP and its effects on biofilm formation and dispersion: a Pseudomonas aeruginosa review. Microbiol. Spectr. 3, MB-0003-2014 (2015). · DOI · Paper page
- Park, S. & Sauer, K. Controlling Biofilm Development Through Cyclic di-GMP Signaling. in Advances in Experimental Medicine and Biology Vol. 1386, 69–94 (Springer, 2022). · DOI
- Hickman, J. W., Tifrea, D. F. & Harwood, C. S. A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc. Natl Acad. Sci. USA 102, 14422–14427 (2005). · DOI · Paper page
- Borlee, B. R. et al. Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix. Mol. Microbiol. 75, 827–842 (2010). · DOI · Paper page
- Moscoso, J. A. et al. The diguanylate cyclase SadC is a central player in Gac/Rsm-mediated biofilm formation in Pseudomonas aeruginosa. J. Bacteriol. 196, 4081–4088 (2014). · DOI
- Caiazza, N. ickyC. & O’Toole, G. eorgeA. SadB is required for the transition from reversible to irreversible attachment during biofilm formation by Pseudomonas aeruginosa PA14. J. Bacteriol. 186, 4476–4485 (2004). · DOI · Paper page
- Caiazza, N. C., Merritt, J. H., Brothers, K. M. & O’Toole, G. A. Inverse regulation of biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J. Bacteriol. 189, 3603–3612 (2007). · DOI · Paper page
- Merritt, J. H., Brothers, K. M., Kuchma, S. L. & O’Toole, G. A. SadC reciprocally influences biofilm formation and swarming motility via modulation of exopolysaccharide production and flagellar function. J. Bacteriol. 189, 8154–8164 (2007). · DOI · Paper page
- Kuchma, S. L. et al. BifA, a cyclic-di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J. Bacteriol. 189, 8165–8178 (2007). · DOI · Paper page
- Baynham, P. J., Ramsey, D. M., Gvozdyev, B. V., Cordonnier, E. M. & Wozniak, D. J. The Pseudomonas aeruginosa ribbon-helix-helix DNA-binding protein AlgZ (AmrZ) controls twitching motility and biogenesis of type IV Pili. J. Bacteriol. 188, 132 (2006). · doi:10.1128/jb.188.1.132-140.2006
- Paris, Z., Fleming, I. M. C. & Alfonzo, J. D. Determinants of tRNA editing and modification: avoiding conundrums, affecting function. Semin. Cell Dev. Biol. 23, 269–274 (2012). · DOI
- García-Contreras, R., Zhang, X. S., Kim, Y. & Wood, T. K. Protein translation and cell death: The role of rare tRNAs in biofilm formation and in activating dormant phage killer genes. PLoS ONE 3, e2394 (2008). · DOI
- Muriel, C. et al. AmrZ is a major determinant of c-di-GMP levels in Pseudomonas fluorescens F113. Sci. Rep. 8, 1–10 (2018). · doi:10.1038/s41598-018-20419-9
- Pryor, E. E. et al. The transcription factor AmrZ utilizes multiple DNA binding modes to recognize activator and repressor sequences of Pseudomonas aeruginosa virulence genes. PLoS Pathog. 8, e1002648 (2012). · DOI
- Jones, C. J. et al. ChIP-seq and RNA-seq reveal an AmrZ-mediated mechanism for cyclic di-GMP synthesis and biofilm development by Pseudomonas aeruginosa. PLoS Pathog. 10, e1003984 (2014). · DOI · Paper page
- Oladosu, V. I., Park, S. & Sauer, K. Flip the switch: the role of FleQ in modulating the transition between the free-living and sessile mode of growth in Pseudomonas aeruginosa. J. Bacteriol. 206, e0036523 (2024). · DOI
- Hou, L., Debru, A., Chen, Q., Bao, Q. & Li, K. AmrZ regulates swarming motility through cyclic di-GMP-dependent motility inhibition and controlling Pel polysaccharide production in Pseudomonas aeruginosa PA14. Front Microbiol. 10, 1847 (2019). · DOI
- Jones, C. J., Ryder, C. R., Mann, E. E. & Wozniak, D. J. AmrZ modulates pseudomonas aeruginosa biofilm architecture by directly repressing transcription of the psl operon. J. Bacteriol. 195, 1637–1644 (2013). · DOI
- Feng, Q. et al. Regulation of Exopolysaccharide Production by ProE, a Cyclic-Di-GMP Phosphodiesterase in Pseudomonas aeruginosa PAO1. Front Microbiol. 11, 1–18 (2020). · DOI
- Roth, S. et al. Identification of protein-protein interactions using a magnetic modulation biosensing system. Sens Actuators B Chem. 303, 127228 (2020). · DOI
- Zhang, H. et al. Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications. Proteins: Struct., Funct., Genet. 40, 86–97 (2000). · doi:10.1002/(sici)1097-0134(20000701)40:1<86::aid-prot100>3.0.co;2-y
- Ghosh, S. & Deutscher, M. P. Oligoribonuclease is an essential component of the mRNA decay pathway. Proc. Natl Acad. Sci. USA 96, 4372–4377 (1999). · DOI · Paper page
- Martínez-Granero, F. et al. The Gac-Rsm and SadB signal transduction pathways converge on AlgU to downregulate motility in Pseudomonas fluorescens. PLoS ONE 7, e31765 (2012). · DOI
- Lapouge, K., Schubert, M., Allain, F. H. T. & Haas, D. Gac/Rsm signal transduction pathway of γ-proteobacteria: From RNA recognition to regulation of social behaviour. Mol. Microbiol. 67, 241–253 (2008). · DOI · Paper page
- Martínez-Granero, F., Redondo-Nieto, M., Vesga, P., Martín, M. & Rivilla, R. AmrZ is a global transcriptional regulator implicated in iron uptake and environmental adaption in P. fluorescens F113. BMC Genomics 15, 237 (2014). · DOI
- Gur, E. & Sauer, R. T. Recognition of misfolded proteins by Lon, a AAA+ protease. Genes Dev. 22, 2267–2277 (2008). · DOI · Paper page
- Mukherjee, S. et al. Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyper flagellation. Proc. Natl Acad. Sci. USA 112, 250–255 (2015). · DOI
- Muriel, C. et al. The diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB. Sci. Rep. 9, 1–9 (2019). · doi:10.1038/s41598-019-44554-z
- Ryder, C., Byrd, M. & Wozniak, D. J. Role of polysaccharides in Pseudomonas aeruginosa biofilm development. Curr. Opin. Microbiol. 10, 644–648 (2007). · DOI · Paper page
- Daniel, E. et al. ATGme: Open-source web application for rare codon identification and custom DNA sequence optimization. BMC Bioinforma. 16, 303 (2015). · DOI
- Winsor, G. L. et al. Enhanced annotations and features for comparing thousands of Pseudomonas genomes in the Pseudomonas genome database. Nucleic Acids Res. 44, D646–D653 (2016). · DOI · Paper page
- Anders, S., Pyl, P. T. & Huber, W. HTSeq-A Python framework to work with high-throughput sequencing data. Bioinformatics 31, 166–169 (2015). · DOI · Paper page
- Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357–359 (2012). · DOI · Paper page
- Love, M. I., Huber, W. & Anders, S. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol. 15, 1–21 (2014). · DOI · Paper page
- Barak, R. & Opatowsky, Y. Expression, derivatization, crystallization and experimental phasing of an extracellular segment of the human Robo1 receptor. Acta Crystallogr Sect. F. Struct. Biol. Cryst. Commun. 69, 771–775 (2013). · DOI
- Walter, T. S. et al. Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14, 1617–1622 (2006). · DOI · Paper page
- Mueller-Dieckmann, C. et al. The status of the macromolecular crystallography beamlines at the European Synchrotron Radiation Facility. Eur. Phys. J. 130, 70 (2015).
- Krug, M., Weiss, M. S., Heinemann, U. & Mueller, U. XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS. J. Appl Crystallogr 45, 568–572 (2012). · DOI · Paper page
- McCoy, A. J. et al. Phaser crystallographic software. J. Appl Crystallogr 40, 658–674 (2007). · DOI · Paper page
- Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr D. Biol. Crystallogr 66, 486–501 (2010). · DOI · Paper page
- Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr D. Biol. Crystallogr 68, 352–367 (2012). · DOI · Paper page
- Joosten, R. P., Joosten, K., Murshudov, G. N. & Perrakis, A. PDB_REDO: constructive validation, more than just looking for errors. Acta Crystallogr D. Biol. Crystallogr 68, 484–496 (2012). · DOI · Paper page
Cited by
Elbehiry, A., Marzouk, E., Edrees, H. M., Ibrahem, M., Alzahrani, S., Anagreyyah, S., Abualola, H., Alghamdi, A., Alzahrani, A., Jaber, M., et al. (2026) · Microorganisms · doi:10.3390/microorganisms14010109 · Cited by 34
Metadata
- Authors
- Ben-David, Y., Sporny, M., Brochin, Y., Piscon, B., Roth, S., Zander, I., Nisani, M., Shoshani, S., Yaron, O., Karako-Lampert, S., Lebenthal-Loinger, I., Danielli, A., Opatowsky, Y., & Banin, E.
- Venue
- npj Biofilms and Microbiomes
- Published
- 2025-05-13
- Volume
- 11
- Issue
- 1
- ISSN
- 2055-5008
- Cited by
- 6
- References
- 1
- Language
- en
- Licence
- creativecommons.org/licenses/by-nc-nd/4.0 (tdm)
- creativecommons.org/licenses/by-nc-nd/4.0 (vor)
- Funders
- Israel Science Foundation (1694/22 and 1125/17)
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- Ben-David, Y., Sporny, M., Brochin, Y., Piscon, B., Roth, S., Zander, I., Nisani, M., Shoshani, S., Yaron, O., Karako-Lampert, S., Lebenthal-Loinger, I., Danielli, A., Opatowsky, Y., & Banin, E. (2025). SadB, a mediator of AmrZ proteolysis and biofilm development in Pseudomonas aeruginosa. npj Biofilms and Microbiomes. https://doi.org/10.1038/s41522-025-00710-0
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