» Articles » PMID: 24451384

Inherent Regulation of EAL Domain-catalyzed Hydrolysis of Second Messenger Cyclic Di-GMP

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2014 Jan 24
PMID 24451384
Citations 35
Authors
Affiliations
Soon will be listed here.
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 with the dimerization affinity being increased about 100-fold upon substrate binding. Crystal structures of the YahA-EAL domain determined under various conditions (apo, Mg(2+), cdG·Ca(2+) complex) confirm structural coupling between the dimer interface and the catalytic center. The built-in regulatory properties of the EAL domain probably facilitate its modular, functional combination with the diverse repertoire of accessory domains.

Citing Articles

Control of phosphodiesterase activity in the regulator of biofilm dispersal RbdA from .

Cordery C, Craddock J, Maly M, Basavaraja K, Webb J, Walsh M RSC Chem Biol. 2024; .

PMID: 39247681 PMC: 11372557. DOI: 10.1039/d4cb00113c.


A genetic switch controls Pseudomonas aeruginosa surface colonization.

Manner C, Teixeira R, Saha D, Kaczmarczyk A, Zemp R, Wyss F Nat Microbiol. 2023; 8(8):1520-1533.

PMID: 37291227 DOI: 10.1038/s41564-023-01403-0.


The role of bacterial signaling networks in antibiotics response and resistance regulation.

Li Y, Feng T, Wang Y Mar Life Sci Technol. 2023; 4(2):163-178.

PMID: 37073223 PMC: 10077285. DOI: 10.1007/s42995-022-00126-1.


Mutant structure of metabolic switch protein in complex with monomeric c-di-GMP reveals a potential mechanism of protein-mediated ligand dimerization.

Dubey B, Shyp V, Fucile G, Sondermann H, Jenal U, Schirmer T Sci Rep. 2023; 13(1):2727.

PMID: 36810577 PMC: 9944927. DOI: 10.1038/s41598-023-29110-0.


Characterisation of sequence-structure-function space in sensor-effector integrators of phytochrome-regulated diguanylate cyclases.

Bohm C, Gourinchas G, Zweytick S, Hujdur E, Reiter M, Trstenjak S Photochem Photobiol Sci. 2022; 21(10):1761-1779.

PMID: 35788917 PMC: 9587094. DOI: 10.1007/s43630-022-00255-7.


References
1.
Navarro M, De N, Bae N, Wang Q, Sondermann H . Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure. 2009; 17(8):1104-16. PMC: 2747306. DOI: 10.1016/j.str.2009.06.010. View

2.
Barends T, Hartmann E, Griese J, Beitlich T, Kirienko N, Ryjenkov D . Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature. 2009; 459(7249):1015-8. DOI: 10.1038/nature07966. View

3.
Paul R, Abel S, Wassmann P, Beck A, Heerklotz H, Jenal U . Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J Biol Chem. 2007; 282(40):29170-7. DOI: 10.1074/jbc.M704702200. View

4.
Wang Z . An exact mathematical expression for describing competitive binding of two different ligands to a protein molecule. FEBS Lett. 1995; 360(2):111-4. DOI: 10.1016/0014-5793(95)00062-e. View

5.
Schmidt A, Ryjenkov D, Gomelsky M . The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J Bacteriol. 2005; 187(14):4774-81. PMC: 1169503. DOI: 10.1128/JB.187.14.4774-4781.2005. View