P6-Liu Xipeng

Study on the metabolic mechanism of the nucleoside messenger c-di-AMP in the piezophilic hyperthermophilic Pyrococcus yayanosii CH1

Lei Feng 1, Feng-Ping Wang 1,2, Xiang Xiao1,2, Xi-Peng Liu 1,2,*

1. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China

2. State Key Laboratory of Ocean Engineering, School of Naval Architecture, Ocean and Civil Engineering, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China.

Nucleoside messenger plays an important role in transferring extracellular signals into cells. In order to understand the possible mechanism of adapting to high temperature, high pressure and other environmental factors in the first isolated obligate piezophilic hyperthermophilic archaeon Pyrococcus yayanosii CH1, we studied the metabolic mechanism of nucleoside messenger molecules, such as c-AMP, c-di-GMP, c-di-AMP, as well as linear nucleotides such as (p)ppGpp. We have found a c-di-AMP messenger molecule hydrolase PYCH17020 and the synthase PYCH00940 encoding gene in the genome. The identification of enzyme activity in vitro showed that PYCH17020 had phosphodiesterase activity (PDE), which could degrade c-di-AMP, c-di-GMP, and c-di-IMP. Meanwhile PYCH17020 also could degrade linear purine dinucleotide into single nucleotide. The activity of PDE exists in the C-terminal DHH-DHHA1 domain, and the N-terminal NAD-binding domain had no obvious effect on the PDE activity. This is the first report for the degradation enzymes for nucleoside messenger molecules in Archaea. It provides important clues for the research of nucleoside signaling molecules in regulating the environmental adaptability in extremophiles.