Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger cyclic di-GMP.

ABSTRACT: The universal second messenger cyclic di-GMP (cdG) is involved in the regulation of a diverse range of cellular processes in bacteria. The intracellular concentration of the dinucleotide is determined by the opposing actions of diguanylate cyclases and cdG-specific phosphodiesterases (PDEs). Whereas most PDEs have accessory domains that are involved in the regulation of their activity, the regulatory mechanism of this class of enzymes has remained unclear. Here, we use biophysical and functional analyses to show that the isolated EAL domain of a PDE from Escherichia coli (YahA) is in a fast thermodynamic monomer-dimer equilibrium, and that the domain is active only in its dimeric state. Furthermore, our data indicate thermodynamic coupling between substrate binding and EAL dimerization wit

SUBMITTER: Sundriyal A 

PROVIDER: S-EPMC3945359 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature