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Published on: June 30, 2016
Tandem GGDEF-EAL Domain Proteins Pleiotropically Modulate c-di-GMP Metabolism Enrolled in Bacterial Cellulose
Tianzhen Zhang1,2, Shiqi Zhang1,2, Yan Wang1,2
1Key Laboratory of Industrial Fermentation Microbiology (Ministry of Education), Tianjin University of Science & Technology, Tianjin 300457, People's Republic of China.
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 Komagataeibacter xylinus 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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