Application of Synthetic Peptide Arrays To Uncover Cyclic Di-GMP Binding Motifs

Journal of Bacteriology
Juliane DüvelSusanne Häussler

Abstract

High levels of the universal bacterial second messenger cyclic di-GMP (c-di-GMP) promote the establishment of surface-attached growth in many bacteria. Not only can c-di-GMP bind to nucleic acids and directly control gene expression, but it also binds to a diverse array of proteins of specialized functions and orchestrates their activity. Since its development in the early 1990s, the synthetic peptide array technique has become a powerful tool for high-throughput approaches and was successfully applied to investigate the binding specificity of protein-ligand interactions. In this study, we used peptide arrays to uncover the c-di-GMP binding site of a Pseudomonas aeruginosa protein (PA3740) that was isolated in a chemical proteomics approach. PA3740 was shown to bind c-di-GMP with a high affinity, and peptide arrays uncovered LKKALKKQTNLR to be a putative c-di-GMP binding motif. Most interestingly, different from the previously identified c-di-GMP binding motif of the PilZ domain (RXXXR) or the I site of diguanylate cyclases (RXXD), two leucine residues and a glutamine residue and not the charged amino acids provided the key residues of the binding sequence. Those three amino acids are highly conserved across PA3740 homologs, an...Continue Reading

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Citations

Sep 1, 2016·Nature Communications·Yu-Chuan WangShan-Ho Chou
Mar 14, 2019·Molecular Microbiology·Sarina BenseJuliane Düvel
Apr 25, 2020·Environmental Microbiology·Guang-Lei MaZhao-Xun Liang
Apr 30, 2016·The Journal of Biological Chemistry·Martina Valentini, Alain Filloux

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