ArticleJournal of bacteriology2011
Homodimerization and binding of specific domains to the target DNA are essential requirements for HlyU to regulate expression of the virulence gene rtxA1, encoding the repeat-in-toxin protein in the human pathogen Vibrio vulnificus.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Increased intracellular persulfide levels attenuate HlyU-mediated hemolysin transcriptional activation inbioRxiv : the preprint server for biology · 2023Article
- The role of Vibrio vulnificus virulence factors and regulators in its infection-induced sepsis.Folia microbiologica · 2020Review
- The Transcriptional Regulator HlyU Positively Regulates Expression ofJournal of bacteriology · 2018Article
- Identification of 2',4'-Dihydroxychalcone as an Antivirulence Agent Targeting HlyU, a Master Virulence Regulator inMolecules (Basel, Switzerland) · 2018Article
- Identification and Validation of an Antivirulence Agent Targeting HlyU-Regulated Virulence inFrontiers in cellular and infection microbiology · 2018Article
- Identification and characterization ofThe Journal of biological chemistry · 2017Article
- Identification of the target DNA sequence and characterization of DNA binding features of HlyU, and suggestion of a redox switch for hlyA expression in the human pathogen Vibrio cholerae from in silico studies.Nucleic acids research · 2015Article
- Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation.The EMBO journal · 2013Article
- The regulator HlyU, the repeat-in-toxin gene rtxA1, and their roles in the pathogenesis of Vibrio vulnificus infections.MicrobiologyOpen · 2012Review
- Regulatory characteristics of the Vibrio vulnificus rtxHCA operon encoding a MARTX toxin.Journal of microbiology (Seoul, Korea) · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The virulence gene rtxA1, encoding the repeat-in-toxin protein, plays an essential role in the pathogenesis of Vibrio vulnificus infections. Expression of this gene is controlled by the HlyU regulator by direct contact of the DNA upstream of the rtxA1 toxin operon acting as a derepressor of the H-NS protein. The crystal structure suggests that HlyU forms a homodimer in vitro. However, knowledge of the biological implications of these findings in vivo is limited. In this work, we endeavored to dissect, using genetic and biochemical approaches, the domains of this protein that are essential for homodimer formation and the interaction of HlyU with the target DNA. We identified that residues L18, N22, R25, S54, Q55, L57, W59, R61, K70, and Y77 are essential for the HlyU protein binding to the DNA and that amino acids L17 and L91 are important for HlyU dimerization. We also determined that HlyU homodimer formation is an essential requirement for binding to the upstream region of the rtxA1 operon and is the key feature in relieving the H-NS repression of rtxA1 transcription.
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