Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure-function studies of Rgg binding to pheromones and target promoters reveal a model of transcription factor interplay.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 117, Issue 39, Page 24494-24502, Year 2020
Publish date	Sep 29, 2020
Authors	Glenn C Capodagli / Kaitlyn M Tylor / Jason T Kaelber / Vasileios I Petrou / Michael J Federle / Matthew B Neiditch /
PubMed Abstract	Regulator gene of glucosyltransferase (Rgg) family proteins, such as Rgg2 and Rgg3, have emerged as primary quorum-sensing regulated transcription factors in species, controlling virulence, ...Regulator gene of glucosyltransferase (Rgg) family proteins, such as Rgg2 and Rgg3, have emerged as primary quorum-sensing regulated transcription factors in species, controlling virulence, antimicrobial resistance, and biofilm formation. Rgg2 and Rgg3 function is regulated by their interaction with oligopeptide quorum-sensing signals called short hydrophobic peptides (SHPs). The molecular basis of Rgg-SHP and Rgg-target DNA promoter specificity was unknown. To close this gap, we determined the cryoelectron microscopy (cryo-EM) structure of Rgg3 bound to its quorum-sensing signal, SHP3, and the X-ray crystal structure of Rgg3 alone. Comparison of these structures with that of an Rgg in complex with cyclosporin A (CsA), an inhibitor of SHP-induced Rgg activity, reveals the molecular basis of CsA function. Furthermore, to determine how Rgg proteins recognize DNA promoters, we determined X-ray crystal structures of both Rgg2 and Rgg3 in complex with their target DNA promoters. The physiological importance of observed Rgg-DNA interactions was dissected using in vivo genetic experiments and in vitro biochemical assays. Based on these structure-function studies, we present a revised unifying model of Rgg regulatory interplay. In contrast to existing models, where Rgg2 proteins are transcriptional activators and Rgg3 proteins are transcriptional repressors, we propose that both are capable of transcriptional activation. However, when Rgg proteins with different activation requirements compete for the same DNA promoters, those with more stringent activation requirements function as repressors by blocking promoter access of SHP-bound conformationally active Rgg proteins. While a similar gene expression regulatory scenario has not been previously described, in all likelihood it is not unique to streptococci.
External links	Proc Natl Acad Sci U S A / PubMed:32907945 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.202 - 3.2 Å
Structure data	22341 7ji0 EMDB-22341, PDB-7ji0: CryoEM structure of Streptococcus thermophilus SHP pheromone receptor Rgg3 in complex with SHP3 Method: EM (single particle) / Resolution: 2.95 Å PDB-6w1a: Crystal structure of Streptococcus dysgalactiae SHP pheromone receptor Rgg2 bound to DNA Method: X-RAY DIFFRACTION / Resolution: 2.8 Å PDB-6w1e: Crystal structure of Streptococcus thermophilus SHP pheromone receptor Rgg3 Method: X-RAY DIFFRACTION / Resolution: 2.202 Å PDB-6w1f: Crystal structure of Streptococcus thermophilus SHP pheromone receptor Rgg3 bound to DNA Method: X-RAY DIFFRACTION / Resolution: 3.2 Å
Chemicals	ChemComp-PO4: PHOSPHATE ION ChemComp-GOL: GLYCEROL ChemComp-HOH: WATER ChemComp-SO4: SULFATE ION
Source	Streptococcus thermophilus (bacteria) streptococcus thermophilus (strain atcc baa-250 / lmg 18311) (bacteria) streptococcus thermophilus cnrz1066 (bacteria) streptococcus dysgalactiae (bacteria)
Keywords	DNA BINDING PROTEIN/DNA / PHEROMONE BINDING / QUORUM SENSING / DNA BINDING PROTEIN / RRNPP / DNA BINDING PROTEIN-DNA complex / TRANSCRIPTIONAL REGULATOR / DNA binding transcription factor