Pseudomonas aeruginosa AmrZ C‐terminal domain mediates tetramerization and is required for its activator and repressor functions

Pseudomonas aeruginosa is an important bacterial opportunistic pathogen, presenting a significant threat towards individuals with underlying diseases such as cystic fibrosis. The transcription factor AmrZ regulates expression of multiple P. aeruginosa virulence factors. AmrZ belongs to the ribbon–he...

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Published inEnvironmental microbiology reports Vol. 8; no. 1; pp. 85 - 90
Main Authors Xu, Binjie, Ju, Yue, Soukup, Randal J, Ramsey, Deborah M, Fishel, Richard, Wysocki, Vicki H, Wozniak, Daniel J
Format Journal Article
LanguageEnglish
Published United States Society for Applied Microbiology and Blackwell Pub 01.02.2016
Blackwell Publishing Ltd
John Wiley & Sons, Inc
Subjects
Cystic fibrosis
DNA
DNA, Bacterial - metabolism
Gene deletion
Gene Expression Regulation, Bacterial
Genetic testing
Mass spectrometry
Motility
Opportunist infection
pathogens
Protein Binding
Protein Interaction Domains and Motifs
Protein Multimerization
Proteins
Pseudomonas aeruginosa
Pseudomonas aeruginosa - genetics
Pseudomonas aeruginosa - metabolism
Scientific imaging
Sequence Deletion
Spectrometry, Mass, Electrospray Ionization
Transcription factors
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - metabolism
virulence
Virulence factors
Virulence Factors - biosynthesis
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Summary:Pseudomonas aeruginosa is an important bacterial opportunistic pathogen, presenting a significant threat towards individuals with underlying diseases such as cystic fibrosis. The transcription factor AmrZ regulates expression of multiple P. aeruginosa virulence factors. AmrZ belongs to the ribbon–helix–helix protein superfamily, in which many members function as dimers, yet others form higher order oligomers. In this study, four independent approaches were undertaken and demonstrated that the primary AmrZ form in solution is tetrameric. Deletion of the AmrZ C‐terminal domain leads to loss of tetramerization and reduced DNA binding to both activated and repressed target promoters. Additionally, the C‐terminal domain is essential for efficient AmrZ‐mediated activation and repression of its targets.
Bibliography:http://dx.doi.org/10.1111/1758-2229.12354
istex:876222A4813F7CC7BB7F152CC4B20E4F2E21524B
Fig. S1. The primary form of AmrZ in solution is tetrameric. Fig. S2. Dominant negative effect of AmrZR22A. Fig. S3. AmrZR22A formed tetramers in solution. Fig. S4. The C-terminal domain of AmrZ is required for tetramerization. Fig. S5. Predicted AmrZ secondary structure and polarity of the AmrZ CTD. Fig. S6. AmrZ1-66 displayed reduced binding affinity to the gcbA promoter. Fig. S7. Western blot analyses of AmrZ1-66 after arabinose induction. Fig. S8. Efficient activation of PalgD requires the AmrZ C-terminal domain. Fig. S9. Alignment of AmrZ with other Arc proteins. Table S1. Strains, plasmids, and oligonucleotides used in this study. Table S2. The AmrZ CTD is required for efficient activation of twitching motility.
ArticleID:EMI412354
Public Health Preparedness for Infectious Diseases
Cystic Fibrosis Foundation - No. XU13H0
ark:/67375/WNG-NFMGM2H5-R
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
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ISSN:1758-2229
1758-2229
DOI:10.1111/1758-2229.12354