scholarly journals Conformational Change-Induced Repeat Domain Expansion Regulates Rap Phosphatase Quorum-Sensing Signal Receptors

PLoS Biology ◽  
2013 ◽  
Vol 11 (3) ◽  
pp. e1001512 ◽  
Author(s):  
Vijay Parashar ◽  
Philip D. Jeffrey ◽  
Matthew B. Neiditch
Keyword(s):  
Quorum Sensing ◽  
Conformational Change ◽  
Repeat Domain ◽  
Signal Receptors

scholarly journals Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox

2021 ◽  
Author(s):  
Nicole R. Rutbeek ◽  
Hanieh Rezasoltani ◽  
Trushar R. Patel ◽  
Mazdak Khajehpour ◽  
Gerd Prehna
Keyword(s):  
Quorum Sensing ◽  
Conformational Change ◽  
Molecular Mechanism ◽  
Streptococcus Pyogenes ◽  
Scattering Data ◽  
Gram Positive ◽  
Quorum Sensing Inhibition ◽  
X Ray ◽  
Phage Protein ◽  
Phage Proteins

Streptococcus pyogenes, or Group A Streptococcus, is a Gram-positive bacterium that can be both a human commensal and pathogen. Central to this dichotomy are temperate bacteriophages that incorporate into the bacterial genome as a prophage. These genetic elements encode both the phage proteins as well as toxins harmful to the human host. One such conserved phage protein paratox (Prx) is always found encoded adjacent to the toxin genes and this linkage is preserved during transduction. Within Streptococcus pyogenes, Prx functions to inhibit the quorum-sensing ComRS receptor-signal pair that is the master regulator of natural competence, or the ability to uptake endogenous DNA. Specifically, Prx directly binds and inhibits the receptor ComR by unknown mechanism. To understand how Prx inhibits ComR at the molecular level we pursued an X-ray crystal structure of Prx bound to ComR. The structural data supported by solution X-ray scattering data demonstrate that Prx induces a conformational change in ComR to directly access the DNA binding domain. Furthermore, electromobility shift assays and competition binding assays reveal that Prx effectively uncouples the inter-domain conformational change that is required for activation of ComR by the signaling molecule XIP. Although to our knowledge the molecular mechanism of quorum-sensing inhibition by Prx is unique, it is analogous to the mechanism employed by the phage protein Aqs1 in Pseudomonas aeruginosa. Together, this demonstrates an example of convergent evolution between Gram-positive and Gram-negative phages to inhibit quorum-sensing, and highlights the versatility of small phage proteins.

scholarly journals Insight in the quorum sensing-driven lifestyle of the non-pathogenic Agrobacterium tumefaciens 6N2 and the interactions with the yeast Meyerozyma guilliermondii

2021 ◽  
Author(s):  
Elisa Violeta Bertini ◽  
Mariela Analia Torres ◽  
Thibaut Leger ◽  
Camille Garcia ◽  
Kar-Wai Hong ◽  
...  
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Quorum Sensing ◽  
Plant Tissues ◽  
Meyerozyma Guilliermondii ◽  
Proteomic Approach ◽  
Dual Cultures ◽  
Yeast Interactions ◽  
Signal Receptors

Agrobacterium tumefaciens is considered a prominent phytopathogen, though most isolates are nonpathogenic. Agrobacteria can inhabit plant tissues interacting with other microorganisms. Yeasts are likewise part of these communities. We analyzed the quorum sensing (QS) systems of A. tumefaciens strain 6N2, and its relevance for the interaction with the yeast Meyerozyma guilliermondii, both sugarcane endophytes. We show that strain 6N2 is nonpathogenic, produces OHC8-HSL, OHC10-HSL, OC12-HSL and OHC12-HSL as QS signals, and possesses a complex QS architecture, with one truncated, two complete systems, and three additional QS-signal receptors. A proteomic approach showed differences in QS-regulated proteins between pure (64 proteins) and dual (33 proteins) cultures. Seven proteins were consistently regulated by quorum sensing in pure and dual cultures. M. guilliermondii proteins influenced by QS activity were also evaluated. Several up- and down- regulated proteins differed depending on the bacterial QS. These results show the importance of the QS regulation in the bacteria-yeast interactions.

2-5A induces a conformational change in the ankyrin-repeat domain of RNase L

2005 ◽  
Vol 60 (1) ◽  
pp. 131-138 ◽  
Author(s):  
Masayuki Nakanishi ◽  
Yoshikuni Goto ◽  
Yukio Kitade
Keyword(s):  
Conformational Change ◽  
Ankyrin Repeat ◽  
Rnase L ◽  
Repeat Domain ◽  
Ankyrin Repeat Domain

scholarly journals Synthesis and application of an N-acylated l-homoserine lactone derivatized affinity matrix for the isolation of quorum sensing signal receptors

2011 ◽  
Vol 21 (17) ◽  
pp. 5054-5057 ◽  
Author(s):  
Thanit Praneenararat ◽  
Teresa M.J. Beary ◽  
Anthony S. Breitbach ◽  
Helen E. Blackwell
Keyword(s):  
Quorum Sensing ◽  
Homoserine Lactone ◽  
Affinity Matrix ◽  
Signal Receptors

scholarly journals The Burkholderia mallei BmaR3-BmaI3 Quorum-Sensing System Produces and Responds to N-3-Hydroxy-Octanoyl Homoserine Lactone

2008 ◽  
Vol 190 (14) ◽  
pp. 5137-5141 ◽  
Author(s):  
Breck A. Duerkop ◽  
Jake P. Herman ◽  
Ricky L. Ulrich ◽  
Mair E. A. Churchill ◽  
E. Peter Greenberg
Keyword(s):  
Escherichia Coli ◽  
Quorum Sensing ◽  
Homoserine Lactone ◽  
Acyl Homoserine Lactone ◽  
Burkholderia Mallei ◽  
E Coli ◽  
Additional Signal ◽  
Sensing System ◽  
Quorum Sensing System ◽  
Signal Receptors

ABSTRACT Burkholderia mallei has two acyl-homoserine lactone (acyl-HSL) signal generator-receptor pairs and two additional signal receptors, all of which contribute to virulence. We show that B. mallei produces N-3-hydroxy-octanoyl HSL (3OHC8-HSL) but a bmaI3 mutant does not. Recombinant Escherichia coli expressing BmaI3 produces hydroxylated acyl-HSLs, with 3OHC8-HSL being the most abundant compound. In recombinant E. coli, BmaR3 responds to 3OHC8-HSL but not to other acyl-HSLs. These data indicate that the signal for BmaR3-BmaI3 quorum sensing is 3OHC8-HSL.

scholarly journals Reversible Conformational Change in the Plasmodium falciparum Circumsporozoite Protein Masks Its Adhesion Domains

2015 ◽  
Vol 83 (10) ◽  
pp. 3771-3780 ◽  
Author(s):  
Raul Herrera ◽  
Charles Anderson ◽  
Krishan Kumar ◽  
Alvaro Molina-Cruz ◽  
Vu Nguyen ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Conformational Change ◽  
Circumsporozoite Protein ◽  
Type I ◽  
Label Free ◽  
Content Type ◽  
C Terminus ◽  
Repeat Domain ◽  
Molecular Signal

The extended rod-likePlasmodium falciparumcircumsporozoite protein (CSP) is comprised of three primary domains: a charged N terminus that binds heparan sulfate proteoglycans, a central NANP repeat domain, and a C terminus containing a thrombospondin-like type I repeat (TSR) domain. Only the last two domains are incorporated in RTS,S, the leading malaria vaccine in phase 3 trials that, to date, protects about 50% of vaccinated children against clinical disease. A seroepidemiological study indicated that the N-terminal domain might improve the efficacy of a new CSP vaccine. Using a panel of CSP-specific monoclonal antibodies, well-characterized recombinant CSPs, label-free quantitative proteomics, andin vitroinhibition of sporozoite invasion, we show that native CSP is N-terminally processed in the mosquito host and undergoes a reversible conformational change to mask some epitopes in the N- and C-terminal domains until the sporozoite interacts with the liver hepatocyte. Our findings show the importance of understanding processing and the biophysical change in conformation, possibly due to a mechanical or molecular signal, and may aid in the development of a new CSP vaccine.

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