Details
| Original language | English |
|---|---|
| Pages (from-to) | 522-34 |
| Number of pages | 13 |
| Journal | Genes & development |
| Volume | 23 |
| Issue number | 4 |
| Publication status | Published - 15 Feb 2009 |
| Externally published | Yes |
Abstract
The blue light using FAD (BLUF)-EAL protein YcgF is a known blue-light sensor of Escherichia coli, but its direct regulatory output and physiological function have remained unknown. Here, we demonstrate that unlike other EAL domain proteins, YcgF does not degrade the signaling molecule c-di-GMP, but directly binds to and releases the MerR-like repressor YcgE from its operator DNA upon blue-light irradiation. As a consequence, a distinct regulon of eight small proteins (of 71-126 amino acids) is strongly induced. These include YmgA and YmgB, which, via the RcsC/RcsD/RcsB two-component phosphorelay system, activate production of the biofilm matrix substance colanic acid as well as acid resistance genes and the biofilm-associated bdm gene and down-regulate adhesive curli fimbriae. Thus, small proteins under YcgF/YcgE control seem to act as "connectors" that provide additional signal input into a two-component signaling pathway. Moreover, we found ycgF and ycgE expression to be strongly activated at low temperature, and we elucidate how blue light, cold, and starvation signals are integrated in the expression and activity of the YcgF/YcgE/small protein signaling pathway. In conclusion, this pathway may modulate biofilm formation via the two-component network when E. coli has to survive in an extrahost aquatic environment.
Keywords
- Bacterial Proteins/antagonists & inhibitors, Biofilms, DNA-Binding Proteins/antagonists & inhibitors, Escherichia coli/metabolism, Escherichia coli Proteins/metabolism, Gene Expression Regulation, Bacterial/radiation effects, Light, Phosphoric Diester Hydrolases/metabolism, Signal Transduction, Stress, Physiological, Temperature
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In: Genes & development, Vol. 23, No. 4, 15.02.2009, p. 522-34.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli
AU - Tschowri, Natalia
AU - Busse, Susan
AU - Hengge, Regine
PY - 2009/2/15
Y1 - 2009/2/15
N2 - The blue light using FAD (BLUF)-EAL protein YcgF is a known blue-light sensor of Escherichia coli, but its direct regulatory output and physiological function have remained unknown. Here, we demonstrate that unlike other EAL domain proteins, YcgF does not degrade the signaling molecule c-di-GMP, but directly binds to and releases the MerR-like repressor YcgE from its operator DNA upon blue-light irradiation. As a consequence, a distinct regulon of eight small proteins (of 71-126 amino acids) is strongly induced. These include YmgA and YmgB, which, via the RcsC/RcsD/RcsB two-component phosphorelay system, activate production of the biofilm matrix substance colanic acid as well as acid resistance genes and the biofilm-associated bdm gene and down-regulate adhesive curli fimbriae. Thus, small proteins under YcgF/YcgE control seem to act as "connectors" that provide additional signal input into a two-component signaling pathway. Moreover, we found ycgF and ycgE expression to be strongly activated at low temperature, and we elucidate how blue light, cold, and starvation signals are integrated in the expression and activity of the YcgF/YcgE/small protein signaling pathway. In conclusion, this pathway may modulate biofilm formation via the two-component network when E. coli has to survive in an extrahost aquatic environment.
AB - The blue light using FAD (BLUF)-EAL protein YcgF is a known blue-light sensor of Escherichia coli, but its direct regulatory output and physiological function have remained unknown. Here, we demonstrate that unlike other EAL domain proteins, YcgF does not degrade the signaling molecule c-di-GMP, but directly binds to and releases the MerR-like repressor YcgE from its operator DNA upon blue-light irradiation. As a consequence, a distinct regulon of eight small proteins (of 71-126 amino acids) is strongly induced. These include YmgA and YmgB, which, via the RcsC/RcsD/RcsB two-component phosphorelay system, activate production of the biofilm matrix substance colanic acid as well as acid resistance genes and the biofilm-associated bdm gene and down-regulate adhesive curli fimbriae. Thus, small proteins under YcgF/YcgE control seem to act as "connectors" that provide additional signal input into a two-component signaling pathway. Moreover, we found ycgF and ycgE expression to be strongly activated at low temperature, and we elucidate how blue light, cold, and starvation signals are integrated in the expression and activity of the YcgF/YcgE/small protein signaling pathway. In conclusion, this pathway may modulate biofilm formation via the two-component network when E. coli has to survive in an extrahost aquatic environment.
KW - Bacterial Proteins/antagonists & inhibitors
KW - Biofilms
KW - DNA-Binding Proteins/antagonists & inhibitors
KW - Escherichia coli/metabolism
KW - Escherichia coli Proteins/metabolism
KW - Gene Expression Regulation, Bacterial/radiation effects
KW - Light
KW - Phosphoric Diester Hydrolases/metabolism
KW - Signal Transduction
KW - Stress, Physiological
KW - Temperature
U2 - 10.1101/gad.499409
DO - 10.1101/gad.499409
M3 - Article
C2 - 19240136
VL - 23
SP - 522
EP - 534
JO - Genes & development
JF - Genes & development
SN - 0890-9369
IS - 4
ER -