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Structure and regulation of EAL domain proteins

Structure and regulation of EAL domain proteins
Structure and regulation of EAL domain proteins
The formation and dispersal of bacterial biofilms is strongly correlated with cellular levels of bis-(3′–5′) cyclic dimeric guanosine monophosphate, cyclic di-GMP, a secondary messenger that has been shown to be involved in regulation of a broad range of cellular processes in bacteria. Diguanylate cyclases (DGCs) are required for synthesis of cyclic di-GMP, with phosphodiesterases (PDEs) responsible for its breakdown. This review focuses on PDEs characterised by the presence of the conserved “EAL” sequence motif. Typically found in multi-domain proteins, EAL domains can couple to sensory or regulatory domains that allow their activity to be regulated by environmental stimuli or cellular cues. Additionally, catalytically inactive EAL PDEs are suggested to have a sensory or otherwise regulatory function. Recent structure determination provides a wealth of information on PDE function and regulation and has provided novel insight into the enzymatic reaction mechanism. Several regulatory layers may control activity, including dimerisation, active site formation, and metal coordination. In this review, we provide a concise summary of these exciting findings and highlight open research questions that will allow us in future to decipher many of the cellular signals responsible for regulation of PDE activity and cellular processes influenced by these pivotal enzymes.
27-48
Springer, Cham
Webb, Jeremy
ec0a5c4e-86cc-4ae9-b390-7298f5d65f8d
Bellini, Dom
39c25764-e748-4639-9df2-197e74083002
Hutchin, Andrew
5659cf31-f52e-451e-9cf0-4e786924d1ae
Soren, Odel
36eafd44-c181-43e5-a9e3-b45fee755749
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Walsh, Martin A.
c51d771b-68b4-4c84-8906-650fc25bdad3
Chou, Shan-Ho
Guiliani, Nicolas
Lee, Vincent
Römling, Ute
Webb, Jeremy
ec0a5c4e-86cc-4ae9-b390-7298f5d65f8d
Bellini, Dom
39c25764-e748-4639-9df2-197e74083002
Hutchin, Andrew
5659cf31-f52e-451e-9cf0-4e786924d1ae
Soren, Odel
36eafd44-c181-43e5-a9e3-b45fee755749
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Walsh, Martin A.
c51d771b-68b4-4c84-8906-650fc25bdad3
Chou, Shan-Ho
Guiliani, Nicolas
Lee, Vincent
Römling, Ute

Webb, Jeremy, Bellini, Dom, Hutchin, Andrew, Soren, Odel, Tews, Ivo and Walsh, Martin A. (2020) Structure and regulation of EAL domain proteins. In, Chou, Shan-Ho, Guiliani, Nicolas, Lee, Vincent and Römling, Ute (eds.) Microbial Cyclic Di-Nucleotide Signaling. 1 ed. Springer, Cham, pp. 27-48. (doi:10.1007/978-3-030-33308-9_2).

Record type: Book Section

Abstract

The formation and dispersal of bacterial biofilms is strongly correlated with cellular levels of bis-(3′–5′) cyclic dimeric guanosine monophosphate, cyclic di-GMP, a secondary messenger that has been shown to be involved in regulation of a broad range of cellular processes in bacteria. Diguanylate cyclases (DGCs) are required for synthesis of cyclic di-GMP, with phosphodiesterases (PDEs) responsible for its breakdown. This review focuses on PDEs characterised by the presence of the conserved “EAL” sequence motif. Typically found in multi-domain proteins, EAL domains can couple to sensory or regulatory domains that allow their activity to be regulated by environmental stimuli or cellular cues. Additionally, catalytically inactive EAL PDEs are suggested to have a sensory or otherwise regulatory function. Recent structure determination provides a wealth of information on PDE function and regulation and has provided novel insight into the enzymatic reaction mechanism. Several regulatory layers may control activity, including dimerisation, active site formation, and metal coordination. In this review, we provide a concise summary of these exciting findings and highlight open research questions that will allow us in future to decipher many of the cellular signals responsible for regulation of PDE activity and cellular processes influenced by these pivotal enzymes.

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Published date: 5 March 2020

Identifiers

Local EPrints ID: 440673
URI: http://eprints.soton.ac.uk/id/eprint/440673
PURE UUID: dcf5291e-cfa7-4bb7-a0f6-934222cacf35
ORCID for Jeremy Webb: ORCID iD orcid.org/0000-0003-2068-8589
ORCID for Ivo Tews: ORCID iD orcid.org/0000-0002-4704-1139

Catalogue record

Date deposited: 13 May 2020 16:34
Last modified: 18 Feb 2021 17:15

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