Details
| Original language | English |
|---|---|
| Pages (from-to) | 893-906 |
| Number of pages | 14 |
| Journal | Molecular microbiology |
| Volume | 85 |
| Issue number | 5 |
| Publication status | Published - Sept 2012 |
| Externally published | Yes |
Abstract
Escherichia coli senses blue light via the BLUF-EAL protein BluF (YcgF). The degenerate EAL domain of BluF does not have cyclic-di-GMP phosphodiesterase activity, but BluF directly antagonizes the MerR-like repressor BluR (YcgE), which leads to expression of the ycgZ-ymgABC operon and activation of the Rcs system (Tschowri et al., 2009; Genes Dev 23: 522-534). While bluR, bluF and ycgZ have individual transcriptional start sites, comparative genome analysis indicates that the bluR-bluF-ycgZ-ymgAB region represents a functional unit in various enteric bacteria that is characterized by bluF alleles encoding degenerate EAL domains. Re-introducing conserved amino acids involved in phosphodiesterase activity of EAL domains did not restore enzymatic activity or c-di-GMP binding of BluF, but weakened its ability to antagonize BluR and improved a residual interaction with the BluR paralogue MlrA, which controls expression of the biofilm regulator CsgD and curli fibres. We identified the BluR binding site in the ycgZ promoter and observed that BluR also has residual affinity for the MlrA-dependent csgD promoter. Altogether, we propose that BluF evolved from a blue light-regulated PDE into a specific antagonist of a duplicate of MlrA that became BluR, which controls not only curli but various biofilm functions via the Ymg/Rcs pathway.
Keywords
- Binding Sites, Biofilms/radiation effects, Electrophoresis, Polyacrylamide Gel, Escherichia coli/genetics, Escherichia coli Proteins/genetics, Evolution, Molecular, Genome, Bacterial/genetics, Immunoblotting, Light, Phosphoric Diester Hydrolases/genetics, Promoter Regions, Genetic/genetics, Protein Binding, Pyrophosphatases/genetics, Signal Transduction/genetics
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Molecular microbiology, Vol. 85, No. 5, 09.2012, p. 893-906.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Molecular function and potential evolution of the biofilm-modulating blue light-signalling pathway of Escherichia coli
AU - Tschowri, Natalia
AU - Lindenberg, Sandra
AU - Hengge, Regine
N1 - © 2012 Blackwell Publishing Ltd.
PY - 2012/9
Y1 - 2012/9
N2 - Escherichia coli senses blue light via the BLUF-EAL protein BluF (YcgF). The degenerate EAL domain of BluF does not have cyclic-di-GMP phosphodiesterase activity, but BluF directly antagonizes the MerR-like repressor BluR (YcgE), which leads to expression of the ycgZ-ymgABC operon and activation of the Rcs system (Tschowri et al., 2009; Genes Dev 23: 522-534). While bluR, bluF and ycgZ have individual transcriptional start sites, comparative genome analysis indicates that the bluR-bluF-ycgZ-ymgAB region represents a functional unit in various enteric bacteria that is characterized by bluF alleles encoding degenerate EAL domains. Re-introducing conserved amino acids involved in phosphodiesterase activity of EAL domains did not restore enzymatic activity or c-di-GMP binding of BluF, but weakened its ability to antagonize BluR and improved a residual interaction with the BluR paralogue MlrA, which controls expression of the biofilm regulator CsgD and curli fibres. We identified the BluR binding site in the ycgZ promoter and observed that BluR also has residual affinity for the MlrA-dependent csgD promoter. Altogether, we propose that BluF evolved from a blue light-regulated PDE into a specific antagonist of a duplicate of MlrA that became BluR, which controls not only curli but various biofilm functions via the Ymg/Rcs pathway.
AB - Escherichia coli senses blue light via the BLUF-EAL protein BluF (YcgF). The degenerate EAL domain of BluF does not have cyclic-di-GMP phosphodiesterase activity, but BluF directly antagonizes the MerR-like repressor BluR (YcgE), which leads to expression of the ycgZ-ymgABC operon and activation of the Rcs system (Tschowri et al., 2009; Genes Dev 23: 522-534). While bluR, bluF and ycgZ have individual transcriptional start sites, comparative genome analysis indicates that the bluR-bluF-ycgZ-ymgAB region represents a functional unit in various enteric bacteria that is characterized by bluF alleles encoding degenerate EAL domains. Re-introducing conserved amino acids involved in phosphodiesterase activity of EAL domains did not restore enzymatic activity or c-di-GMP binding of BluF, but weakened its ability to antagonize BluR and improved a residual interaction with the BluR paralogue MlrA, which controls expression of the biofilm regulator CsgD and curli fibres. We identified the BluR binding site in the ycgZ promoter and observed that BluR also has residual affinity for the MlrA-dependent csgD promoter. Altogether, we propose that BluF evolved from a blue light-regulated PDE into a specific antagonist of a duplicate of MlrA that became BluR, which controls not only curli but various biofilm functions via the Ymg/Rcs pathway.
KW - Binding Sites
KW - Biofilms/radiation effects
KW - Electrophoresis, Polyacrylamide Gel
KW - Escherichia coli/genetics
KW - Escherichia coli Proteins/genetics
KW - Evolution, Molecular
KW - Genome, Bacterial/genetics
KW - Immunoblotting
KW - Light
KW - Phosphoric Diester Hydrolases/genetics
KW - Promoter Regions, Genetic/genetics
KW - Protein Binding
KW - Pyrophosphatases/genetics
KW - Signal Transduction/genetics
U2 - 10.1111/j.1365-2958.2012.08147.x
DO - 10.1111/j.1365-2958.2012.08147.x
M3 - Article
C2 - 22783906
VL - 85
SP - 893
EP - 906
JO - Molecular microbiology
JF - Molecular microbiology
SN - 0950-382X
IS - 5
ER -