AI Article Synopsis
- Cyclic diguanosine monophosphate (c-di-GMP) plays a vital role in regulating the synthesis of bacterial cellulose (BC) and is managed by enzymes known as diguanylate cyclases (DGCs) and phosphodiesterases (PDEs).
- A study analyzed ten proteins with GGDEF-EAL tandem domains, revealing five with DGC activity and five with PDE activity, with one protein (GE03) displaying both functions.
- Mutant strains lacking GGDEF-EAL proteins showed significant changes in BC production, while knocking out PDE proteins resulted in a 48.1% increase in BC titer, enhancing the understanding of c-di-GMP's role in BC
Article Abstract
Cyclic diguanosine monophosphate (c-di-GMP) is a crucial secondary messenger that regulates bacterial cellulose (BC) synthesis. It is synthesized by diguanylate cyclase (DGC) containing a Gly-Gly-Asp/Glu-Glu-Phe (GGDEF) domain and degraded by phosphodiesterase (PDE) with a Glu-Ala-Leu (EAL) domain. In this work, a systematic analysis of ten GGDEF-EAL tandem domain proteins from CGMCC 2955 assessed their c-di-GMP metabolic functions and effects on BC titer and structure. Of these, five proteins exhibited DGC activity, and five exhibited PDE activity in vitro. GE03 was identified as a bifunctional protein. Most mutant strains deficient in GGDEF-EAL protein showed changes in BC metabolism, motility, and c-di-GMP levels. The combined knockout of identified PDE proteins increased the BC titer by 48.1% compared to the wild type. Overall, our findings advance our understanding of c-di-GMP signaling and its role in BC synthesis, introducing novel concepts and effective strategies for enhancing industrial BC production.
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| http://dx.doi.org/10.1021/acs.jafc.4c07301 | DOI Listing |
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