| 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. |
