Open AccessNitric oxide controls c-di-GMP turnover in Dinoroseobacter shibae
Author(s) -
Patricia Bedrunka,
Fabien Olbrisch,
Martina Rüger,
Susanne Zehner,
Nicole FrankenbergDinkel
Publication year - 2018
Publication title -
microbiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.352
H-Index - 35
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/mic.0.000714
Subject(s) - nitric oxide , nos1 , signal transduction , microbiology and biotechnology , chemistry , biochemistry , biology , second messenger system , enzyme , nitric oxide synthase , endocrinology
The ubiquitous bacterial second messenger bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) is involved in the regulation of numerous processes including biofilm formation, motility, virulence, cell cycle and differentiation. In this study, we searched the genome of the ecologically important marine alphaproteobacterium Dinoroseobacter shibae DFL12 T for genes encoding putative c-di-GMP-modulating enzymes. Overall, D. shibae was found to possess two diguanylate cyclases (Dshi_2814 and Dshi_2820) as well as two c-di-GMP-specific phosphodiesterases (Dhi_0329 and Dshi_3065). Recombinant expression and purification followed by enzymatic analysis revealed that all four proteins exhibit their proposed activity. Furthermore, adjacent to Dshi_2814 we identified a gene encoding a heme nitric oxide/oxygen binding (H-NOX) protein. These proteins are often found in association with c-di-GMP signal transduction pathways and modulate their function through binding of diatomic gases such as nitric oxide. Here, we demonstrate that H-NOX constitutes a functional unit together with the diguanylate cyclase Dshi_2814. NO-bound H-NOX strongly inhibits DGC activity. Based on these results, and with respect to previously published data including micro-array analysis, we propose an interlinkage of c-di-GMP signalling with cell-cell communication and differentiation in D. shibae.