The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli

authored by: Natalia Tschowri, Susan Busse, Regine Hengge
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.
External Organisation(s): Freie Universität Berlin (FU Berlin)
Type: Article
Journal: Genes & development
Volume: 23
Pages: 522-34
No. of pages: 13
ISSN: 0890-9369
Publication date: 15.02.2009
Publication status: Published
Peer reviewed: Yes
Electronic version(s): https://doi.org/10.1101/gad.499409 (Access: Unknown)

BibTeX

@article{0e77bb511e5141a3a2850934b12fb3f2,
title = "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli",
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",
author = "Natalia Tschowri and Susan Busse and Regine Hengge",
year = "2009",
month = feb,
day = "15",
doi = "10.1101/gad.499409",
language = "English",
volume = "23",
pages = "522--34",
journal = "Genes & development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "4",
}