TY - JOUR
T1 - Dependence of DNA length on binding affinity between TrpR and trpO of DNA
AU - Shimamoto, Nobuo
AU - Toda, Mikito
AU - Nara, Shigetoshi
AU - Komatsuzaki, Tamiki
AU - Kamagata, Kiyoto
AU - Kinebuchi, Takashi
AU - Tomizawa, Jun ichi
N1 - Funding Information:
This work was supported by JSPS (Nos. 25287105, 25650044 to TK, 22654047, 25610105, 19K03653 to MT), and the Research Program of ‘Five’ star Alliance’ in ‘NJRC Matter and Dev.’ (TK,KK,MT,SN). Institute for Chemical Reaction Design and Discovery (ICReDD) was established by WPI, MEXT, Japan. Also, one of the author (SN) appreciates MEXT-JSPS KAKENHI Grant Number JP24120707. The authors thank the anonymous referees for valuable comments. They have led us to correct mistakes in the original manuscript and to improve our explanation for the results. The authors also thank Dr. James Nicholas Taylor at Hokkaido University for checking and suggesting English expressions.
Publisher Copyright:
© 2020, The Author(s).
PY - 2020/12/1
Y1 - 2020/12/1
N2 - We scrutinize the length dependency of the binding affinity of bacterial repressor TrpR protein to trpO (specific site) on DNA. A footprinting experiment shows that the longer the DNA length, the larger the affinity of TrpR to the specific site on DNA. This effect termed “antenna effect” might be interpreted as follows: longer DNA provides higher probability for TrpR to access to the specific site aided by one-dimensional diffusion along the nonspecific sites of DNA. We show that, however, the antenna effect cannot be explained while detailed balance holds among three kinetic states, that is, free protein/DNA, nonspecific complexes, and specific complex. We propose a working hypothesis that slow degree(s) of freedom in the system switch(es) different potentials of mean force causing transitions among the three states. This results in a deviation from detailed balance on the switching timescale. We then derive a simple reaction diffusion/binding model that describes the antenna effect on TrpR binding to its target operator. Possible scenarios for such slow degree(s) of freedom in TrpR–DNA complex are addressed.
AB - We scrutinize the length dependency of the binding affinity of bacterial repressor TrpR protein to trpO (specific site) on DNA. A footprinting experiment shows that the longer the DNA length, the larger the affinity of TrpR to the specific site on DNA. This effect termed “antenna effect” might be interpreted as follows: longer DNA provides higher probability for TrpR to access to the specific site aided by one-dimensional diffusion along the nonspecific sites of DNA. We show that, however, the antenna effect cannot be explained while detailed balance holds among three kinetic states, that is, free protein/DNA, nonspecific complexes, and specific complex. We propose a working hypothesis that slow degree(s) of freedom in the system switch(es) different potentials of mean force causing transitions among the three states. This results in a deviation from detailed balance on the switching timescale. We then derive a simple reaction diffusion/binding model that describes the antenna effect on TrpR binding to its target operator. Possible scenarios for such slow degree(s) of freedom in TrpR–DNA complex are addressed.
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U2 - 10.1038/s41598-020-71598-3
DO - 10.1038/s41598-020-71598-3
M3 - Article
C2 - 32973254
AN - SCOPUS:85091437787
SN - 2045-2322
VL - 10
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 15624
ER -