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Title:A cyclic di-GMP network is present in gram-positive Streptococcus and gram-negative Proteus species
Authors:ID Liu, Ying (Author)
ID Lee, Changhan (Author)
ID Li, Fengyang (Author)
ID Trček, Janja (Author)
ID Bähre, Heike (Author)
ID Guo, Rey-Ting (Author)
ID Chen, Chun-Chi (Author)
ID Chernobrovkin, Alexey (Author)
ID Zubarev, Roman (Author)
ID Römling, Ute (Author)
Files:.pdf Liu-2020-A_Cyclic_di-GMP_Network_Is_Present_in.pdf (12,81 MB)
MD5: 41414C994CBDAC560E036A1412DE4F55
 
URL https://pubs.acs.org/doi/10.1021/acsinfecdis.0c00314
 
Language:English
Work type:Scientific work
Typology:1.01 - Original Scientific Article
Organization:FNM - Faculty of Natural Sciences and Mathematics
Abstract:The ubiquitous cyclic di-GMP (c-di-GMP) network is highly redundant with numerous GGDEF domain proteins as diguanylate cyclases and EAL domain proteins as c-di-GMP specific phosphodiesterases comprising those domains as two of the most abundant bacterial domain superfamilies. One hallmark of the c-di-GMP network is its exalted plasticity as c-di-GMP turnover proteins can rapidly vanish from species within a genus and possess an above average transmissibility. To address the evolutionary forces of c-di-GMP turnover protein maintenance, conservation, and diversity, we investigated a Gram-positive and a Gram-negative species, which preserved only one single clearly identifiable GGDEF domain protein. Species of the family Morganellaceae of the order Enterobacterales exceptionally show disappearance of the c-di-GMP signaling network, but Proteus spp. still retained one diguanylate cyclase. As another example, in species of the bovis, pyogenes, and salivarius subgroups as well as Streptococcus suis and Streptococcus henryi of the genus Streptococcus, one candidate diguanylate cyclase was frequently identified. We demonstrate that both proteins encompass PAS (Per-ARNT-Sim)-GGDEF domains, possess diguanylate cyclase catalytic activity, and are suggested to signal via a PilZ receptor domain at the C-terminus of type 2 glycosyltransferase constituting BcsA cellulose synthases and a cellulose synthase-like protein CelA, respectively. Preservation of the ancient link between production of cellulose(-like) exopolysaccharides and c-di-GMP signaling indicates that this functionality is even of high ecological importance upon maintenance of the last remnants of a c-di-GMP signaling network in some of today’s free-living bacteria.
Keywords:cellulose biosynthesis, cyclic di-GMP signaling, EAL domain, GGDEF domain, Proteus mirabilis, Streptococcus gallolyticus subsp. gallolyticus
Publication status:Published
Publication version:Version of Record
Submitted for review:14.05.2020
Publication date:06.08.2020
Publisher:ACS Publications
Year of publishing:2020
Number of pages:Str. 2672-2687
Numbering:Letn. 6, št. 10
PID:20.500.12556/DKUM-91686 New window
UDC:579
ISSN on article:2373-8227
COBISS.SI-ID:27348995 New window
DOI:10.1021/acsinfecdis.0c00314 New window
Publication date in DKUM:28.01.2025
Views:135
Downloads:19
Metadata:XML DC-XML DC-RDF
Categories:Misc.
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Record is a part of a journal

Title:ACS infectious diseases
Shortened title:ACS infect. dis.
Publisher:ACS Publications
ISSN:2373-8227
COBISS.SI-ID:520515865 New window

Document is financed by a project

Funder:Other - Other funder or multiple funders
Project number:2017-04465
Name:Natural Sciences and Engineering

Licences

License:CC BY 4.0, Creative Commons Attribution 4.0 International
Link:http://creativecommons.org/licenses/by/4.0/
Description:This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Licensing start date:06.08.2020

Secondary language

Language:Slovenian
Keywords:biosinteza celuloze, Proteus mirabilis, Streptococcus gallolyticus subsp. gallolyticus, mikrobiologija, bakterije


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