DNA binding activity of Anabaena sensory rhodopsin transducer probed by fluorescence correlation spectroscopy

Bioscience, Biotechnology, and Biochemistry
Sung Hyun KimDoseok Kim

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, K(D), 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.

References

Nov 1, 1976·Biophysical Journal·D E KoppelW W Webb
Jun 21, 1994·Proceedings of the National Academy of Sciences of the United States of America·M Eigen, R Rigler
Mar 8, 2003·Molecular Microbiology·Kwang-Hwan JungJohn L Spudich
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Jun 21, 2011·Journal of Molecular Biology·Shenlin WangLeonid S Brown
Jan 3, 2012·Biophysical Journal·Elliot L Elson
May 7, 2014·Molecular Microbiology·So Young KimKwang-Hwan Jung

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Methods Mentioned

BETA
fluorescence correlation spectroscopy
FCS
confocal microscopy

Software Mentioned

LabView
FCS

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