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PubMed:26265469 JSONTXT 21 Projects

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Id Subject Object Predicate Lexical cue
T1 0-110 Sentence denotes Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP.
T2 111-294 Sentence denotes The widespread second messenger molecule cyclic di-GMP (cdG) regulates the transition from motile and virulent lifestyles to sessile, biofilm-forming ones in a wide range of bacteria.
T3 295-397 Sentence denotes Many pathogenic and commensal bacterial-host interactions are known to be controlled by cdG signaling.
T4 398-597 Sentence denotes Although the biochemistry of cyclic dinucleotide metabolism is well understood, much remains to be discovered about the downstream signaling pathways that induce bacterial responses upon cdG binding.
T5 598-821 Sentence denotes As part of our ongoing research into the role of cdG signaling in plant-associated Pseudomonas species, we carried out an affinity capture screen for cdG binding proteins in the model organism Pseudomonas fluorescens SBW25.
T6 822-1004 Sentence denotes The flagella export AAA+ ATPase FliI was identified as a result of this screen and subsequently shown to bind specifically to the cdG molecule, with a KD in the low micromolar range.
T7 1005-1072 Sentence denotes The interaction between FliI and cdG appears to be very widespread.
T8 1073-1250 Sentence denotes In addition to FliI homologs from diverse bacterial species, high affinity binding was also observed for the type III secretion system homolog HrcN and the type VI ATPase ClpB2.
T9 1251-1331 Sentence denotes The addition of cdG was shown to inhibit FliI and HrcN ATPase activity in vitro.
T10 1332-1554 Sentence denotes Finally, a combination of site-specific mutagenesis, mass spectrometry, and in silico analysis was used to predict that cdG binds to FliI in a pocket of highly conserved residues at the interface between two FliI subunits.
T11 1555-1746 Sentence denotes Our results suggest a novel, fundamental role for cdG in controlling the function of multiple important bacterial export pathways, through direct allosteric control of export ATPase proteins.