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Abstract
Anabaena sensory rhodopsin transducer (ASRT) is believed to be a major player in the photo-signal transduction cascade, which is triggered by Anabaena sensory rhodopsin. Here, we characterized DNA binding activity of ASRT probed by using fluorescence correlation spectroscopy. We observed clear decrease of diffusion coefficient of DNA upon binding of ASRT. The dissociation constant, KD, of ASRT to 20 bp-long DNA fragments lied in micro-molar range and varied moderately with DNA sequence. Our results suggest that ASRT may interact with several different regions of DNA with different binding affinity for global regulation of several genes that need to be activated depending on the light illumination.
Graphical abstract
By using fluorescence correlation spectroscopy, we characterized DNA sequence dependent binding activity of Anabaena sensory rhodopsin transducer.
Acknowledgments
This work was supported by the Sogang University Research Grant of 2014 (201410043.01). KHJ acknowledges support by National Nuclear R&D Program funded by the Ministry of Science ICT & future planning (2012055325).
Notes
Abbreviations: ASR, Anabaena sensory rhodopsin; ASRT, Anabaena sensory rhodopsin transducer; BSA, bovine serum albumin; FCS, fluorescence correlation spectroscopy; PEC, phycoerythrocyanin.