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

ABSTRACT:

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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

SUBMITTER: Duvel J 

PROVIDER: S-EPMC4686192 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature