Tlr0485 is a cAMP-activated c-di-GMP phosphodiesterase in a cyanobacterium <i>Thermosynechococcus</i>

  • Enomoto Gen
    Department of Life Sciences (Biology), Graduate School of Arts and Sciences, The University of Tokyo Institute for Biology III, Faculty of Biology, University of Freiburg
  • Kamiya Ayako
    Department of Life Sciences (Biology), Graduate School of Arts and Sciences, The University of Tokyo
  • Okuda Yukiko
    Department of Life Sciences (Biology), Graduate School of Arts and Sciences, The University of Tokyo
  • Narikawa Rei
    Core Research for Evolutional Science and Technology, Japan Science and Technology Agency Department of Biological Science, Faculty of Science, Shizuoka University
  • Ikeuchi Masahiko
    Department of Life Sciences (Biology), Graduate School of Arts and Sciences, The University of Tokyo Core Research for Evolutional Science and Technology, Japan Science and Technology Agency Faculty of Education and Integrated Arts and Sciences, Waseda University

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Abstract

<p>Second messenger molecules are crucial components of environmental signaling systems to integrate multiple inputs and elicit physiological responses. Among various kinds of second messengers, cyclic nucleotides cAMP and cyclic di-GMP (c-di-GMP) play pivotal roles in bacterial environmental responses. However, how these signaling systems are interconnected for a concerted regulation of cellular physiology remains elusive. In a thermophilic cyanobacterium Thermosynechococcus vulcanus strain RKN, incident light color is sensed by cyanobacteriochrome photoreceptors to transduce the light information to the levels of c-di-GMP, which induces cellular aggregation probably via cellulose synthase activation. Herein, we identified that Tlr0485, which is composed of a cGMP-specific phosphodiesterases, adenylate cyclases, and FhlA (GAF) domain and an HD-GYP domain, is a cAMP-activated c-di-GMP phosphodiesterase. We also show biochemical evidence that the two class-III nucleotide cyclases, Cya1 and Cya2, are both adenylate cyclases to produce cAMP in T. vulcanus. The prevalence of cAMP-activated c-di-GMP phosphodiesterase genes in cyanobacterial genomes suggests that the direct crosstalk between cAMP and c-di-GMP signaling systems may be crucial for cyanobacterial environmental responses.</p>

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