Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 373, Issue 1, Pages 11-26Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.07.037
Keywords
biofilm; protein structure; gene regulatory protein; acid resistance; E. coli
Categories
Funding
- NIBIB NIH HHS [R01 EB003872, EB 003872-01A1, R01 EB003872-04] Funding Source: Medline
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The Escherichia coli gene cluster ymgABC was identified in transcriptome studies to have a role in biofilm development and stability. In this study, we showed that YmgB represses biofilm formation in rich medium containing glucose, decreases cellular motility, and protects the cell from acid indicating that YmgB has a major role in acid-resistance in E. coli. Our data show that these phenotypes are potentially mediated through interactions with the important cell signal indole. In addition, gel mobility-shift assays suggest that YmgB may be a non-specific DNA-binding protein. Using nickel-enrichment DNA microarrays, we showed that YmgB binds, either directly or indirectly, via a probable ligand, genes important for biofilm formation. To advance our understanding of the function of YmgB, we used X-ray crystallography to solve the structure of the protein to 1.8 angstrom resolution. YmgB is a biological dimer that is structurally homologous to the E. coli gene regulatory protein Hha, despite having only 5% sequence identity. This supports our DNA microarray data showing that YmgB is a gene regulatory protein. Therefore, this protein, which clearly has a critical role in acid-resistance in E. coli, has been renamed as AriR for (r) under bar egulator of (a) under bar cid (r) under bar esistance influenced by indole. (C) 2007 Elsevier Ltd. All rights reserved.
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