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Cyanobacteriochrome SesA is a diguanylate cyclase that induces cell aggregation in Thermosynechococcus.

Authors :
Enomoto G
Nomura R
Shimada T
Ni-Ni-Win
Narikawa R
Ikeuchi M
Source :
The Journal of biological chemistry [J Biol Chem] 2014 Sep 05; Vol. 289 (36), pp. 24801-9. Date of Electronic Publication: 2014 Jul 24.
Publication Year :
2014

Abstract

Cyanobacteria have unique photoreceptors, cyanobacteriochromes, that show diverse spectral properties to sense near-UV/visible lights. Certain cyanobacteriochromes have been shown to regulate cellular phototaxis or chromatic acclimation of photosynthetic pigments. Some cyanobacteriochromes have output domains involved in bacterial signaling using a second messenger cyclic dimeric GMP (c-di-GMP), but its role in cyanobacteria remains elusive. Here, we characterize the recombinant Tlr0924 from a thermophilic cyanobacterium Thermosynechococcus elongatus, which was expressed in a cyanobacterial system. The protein reversibly photoconverts between blue- and green-absorbing forms, which is consistent with the protein prepared from Escherichia coli, and has diguanylate cyclase activity, which is enhanced 38-fold by blue light compared with green light. Therefore, Tlr0924 is a blue light-activated diguanylate cyclase. The protein's relatively low affinity (10.5 mM) for Mg(2+), which is essential for diguanylate cyclase activity, suggests that Mg(2+) might also regulate c-di-GMP signaling. Finally, we show that blue light irradiation under low temperature is responsible for Thermosynechococcus vulcanus cell aggregation, which is abolished when tlr0924 is disrupted, suggesting that Tlr0924 mediates blue light-induced cell aggregation by producing c-di-GMP. Given our results, we propose the name "sesA (sessility-A)" for tlr0924. This is the first report for cyanobacteriochrome-dependent regulation of a sessile/planktonic lifestyle in cyanobacteria via c-di-GMP.<br /> (© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.)

Details

Language :
English
ISSN :
1083-351X
Volume :
289
Issue :
36
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
25059661
Full Text :
https://doi.org/10.1074/jbc.M114.583674