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A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF.

Rogov VV, Rogova NY, Bernhard F, Löhr F, Dötsch V
J Biol Chem 286 18775-83 (2011)
Cited: 24 times
EuropePMC logo PMID: 21471196

Abstract

RcsF, a proposed auxiliary regulator of the regulation of capsule synthesis (rcs) phosphorelay system, is a key element for understanding the RcsC-D-A/B signaling cascade, which is responsible for the regulation of more than 100 genes and is involved in cell division, motility, biofilm formation, and virulence. The RcsC-D-A/B system is one of the most complex bacterial signal transduction pathways, consisting of several membrane-bound and soluble proteins. RcsF is a lipoprotein attached to the outer membrane and plays an important role in activating the RcsC-d-A/B pathway. The exact mechanism of activation of the rcs phosphorelay by RcsF, however, remains unknown. We have analyzed the sequence of RcsF and identified three structural elements: 1) an N-terminal membrane-anchored helix (residues 3-13), 2) a loop (residues 14-48), and 3) a C-terminal folded domain (residues 49-134). We have determined the structure of this C-terminal domain and started to investigate its interaction with potential partners. Important features of its structure are two disulfide bridges between Cys-74 and Cys-118 and between Cys-109 and Cys-124. To evaluate the importance of this RcsF disulfide bridge network in vivo, we have examined the ability of the full-length protein and of specific Cys mutants to initiate the rcs signaling cascade. The results indicate that the Cys-74/Cys-118 and the Cys-109/Cys-124 residues correlate pairwise with the activity of RcsF. Interaction studies showed a weak interaction with an RNA hairpin. However, no interaction could be detected with reagents that are believed to activate the rcs phosphorelay, such as lysozyme, glucose, or Zn(2+) ions.

Reviews - 2l8y mentioned but not cited (1)

  1. Major Tom to Ground Control: How Lipoproteins Communicate Extracytoplasmic Stress to the Decision Center of the Cell. Laloux G, Collet JF. J Bacteriol 199 e00216-17 (2017)

Articles - 2l8y mentioned but not cited (5)

  1. Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins. Konovalova A, Perlman DH, Cowles CE, Silhavy TJ. Proc Natl Acad Sci U S A 111 E4350-8 (2014)
  2. Communication across the bacterial cell envelope depends on the size of the periplasm. Asmar AT, Ferreira JL, Cohen EJ, Cho SH, Beeby M, Hughes KT, Collet JF. PLoS Biol 15 e2004303 (2017)
  3. A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF. Rogov VV, Rogova NY, Bernhard F, Löhr F, Dötsch V. J Biol Chem 286 18775-18783 (2011)
  4. Defining the function of OmpA in the Rcs stress response. Dekoninck K, Létoquart J, Laguri C, Demange P, Bevernaegie R, Simorre JP, Dehu O, Iorga BI, Elias B, Cho SH, Collet JF. Elife 9 e60861 (2020)
  5. Structural and functional characterization of DUF1471 domains of Salmonella proteins SrfN, YdgH/SssB, and YahO. Eletsky A, Michalska K, Houliston S, Zhang Q, Daily MD, Xu X, Cui H, Yee A, Lemak A, Wu B, Garcia M, Burnet MC, Meyer KM, Aryal UK, Sanchez O, Ansong C, Xiao R, Acton TB, Adkins JN, Montelione GT, Joachimiak A, Arrowsmith CH, Savchenko A, Szyperski T, Cort JR. PLoS One 9 e101787 (2014)


Reviews citing this publication (4)

  1. The Complex Rcs Regulatory Cascade. Wall E, Majdalani N, Gottesman S. Annu Rev Microbiol 72 111-139 (2018)
  2. New Insights into the Non-orthodox Two Component Rcs Phosphorelay System. Guo XP, Sun YC. Front Microbiol 8 2014 (2017)
  3. The Rcs System in Enterobacteriaceae: Envelope Stress Responses and Virulence Regulation. Meng J, Young G, Chen J. Front Microbiol 12 627104 (2021)
  4. Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria. Cho SH, Dekoninck K, Collet JF. J Microbiol 61 317-329 (2023)

Articles citing this publication (14)

  1. Lpp, the Braun lipoprotein, turns 50-major achievements and remaining issues. Asmar AT, Collet JF. FEMS Microbiol Lett 365 (2018)
  2. Effects of Lipopolysaccharide Core Sugar Deficiency on Colanic Acid Biosynthesis in Escherichia coli. Ren G, Wang Z, Li Y, Hu X, Wang X. J Bacteriol 198 1576-1584 (2016)
  3. Structural insight into the formation of lipoprotein-β-barrel complexes. Rodríguez-Alonso R, Létoquart J, Nguyen VS, Louis G, Calabrese AN, Iorga BI, Radford SE, Cho SH, Remaut H, Collet JF. Nat Chem Biol 16 1019-1025 (2020)
  4. Structural Basis of the Subcellular Topology Landscape of Escherichia coli. Loos MS, Ramakrishnan R, Vranken W, Tsirigotaki A, Tsare EP, Zorzini V, Geyter J, Yuan B, Tsamardinos I, Klappa M, Schymkowitz J, Rousseau F, Karamanou S, Economou A. Front Microbiol 10 1670 (2019)
  5. Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. Chng SS, Dutton RJ, Denoncin K, Vertommen D, Collet JF, Kadokura H, Beckwith J. Mol Microbiol 85 996-1006 (2012)
  6. High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function. Tata M, Kumar S, Lach SR, Saha S, Hart EM, Konovalova A. Proc Natl Acad Sci U S A 118 e2100369118 (2021)
  7. Importance of the proline-rich region for the regulatory function of RcsF, an outer membrane lipoprotein component of the Escherichia coli Rcs signal transduction system. Umekawa M, Miyagawa H, Kondo D, Matsuoka S, Matsumoto K, Hara H. Microbiology (Reading) 159 1818-1827 (2013)
  8. Role of the inner-membrane histidine kinase RcsC and outer-membrane lipoprotein RcsF in the activation of the Rcs phosphorelay signal transduction system in Escherichia coli. Sato T, Takano A, Hori N, Izawa T, Eda T, Sato K, Umekawa M, Miyagawa H, Matsumoto K, Muramatsu-Fujishiro A, Matsumoto K, Matsuoka S, Hara H. Microbiology (Reading) 163 1071-1080 (2017)
  9. A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System. Pucciarelli MG, Rodríguez L, García-Del Portillo F. Front Microbiol 8 2605 (2017)
  10. Envelope Stress and Regulation of the Salmonella Pathogenicity Island 1 Type III Secretion System. Palmer AD, Slauch JM. J Bacteriol 202 e00272-20 (2020)
  11. Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope. Lach SR, Kumar S, Kim S, Im W, Konovalova A. PLoS Genet 19 e1010601 (2023)
  12. A frameshift in Yersinia pestis rcsD alters canonical Rcs signalling to preserve flea-mammal plague transmission cycles. Guo XP, Yan HQ, Yang W, Yin Z, Vadyvaloo V, Zhou D, Sun YC. Elife 12 e83946 (2023)
  13. Antivirulence DsbA inhibitors attenuate Salmonella enterica serovar Typhimurium fitness without detectable resistance. Dhouib R, Vagenas D, Hong Y, Verderosa AD, Martin JL, Heras B, Totsika M. FASEB Bioadv 3 231-242 (2021)
  14. Altering Escherichia coli envelope integrity by mimicking the lipoprotein RcsF. TagElDein MA, Mohamed NG, Shahein YE, Ziko L, Hussein NA. Arch Microbiol 206 12 (2023)


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