TY - JOUR
T1 - Structure and Function of the Escherichia coli Protein YmgB
T2 - A Protein Critical for Biofilm Formation and Acid-resistance
AU - Lee, Jintae
AU - Page, Rebecca
AU - García-Contreras, Rodolfo
AU - Palermino, Jeanne Marie
AU - Zhang, Xue Song
AU - Doshi, Ojus
AU - Wood, Thomas K.
AU - Peti, Wolfgang
N1 - Funding Information:
This research was supported by the NIH (EB003872-0IAI) to T.K.W. and Brown University start-up funds to W.P. and to R.P. The authors thank D. Reid for help with a portion of the crystallization experiments, and G. Stetson with protein purification. W.P. is the Manning Assistant Professor for Medical Science at Brown University. We are grateful for the gift of E. coli mutants and plasmids by the National Institute of Genetics, Japan.
PY - 2007/10/12
Y1 - 2007/10/12
N2 - 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 Å 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 regulator of acid resistance influenced by indole.
AB - 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 Å 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 regulator of acid resistance influenced by indole.
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U2 - 10.1016/j.jmb.2007.07.037
DO - 10.1016/j.jmb.2007.07.037
M3 - Article
C2 - 17765265
AN - SCOPUS:34548598563
SN - 0022-2836
VL - 373
SP - 11
EP - 26
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -