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Recognition of different DNA sequences by a DNA‐binding protein alters protein dynamics differentially
Author(s) -
Mondol Tanumoy,
Batabyal Subrata,
Mazumder Abhishek,
Roy Siddhartha,
Pal Samir Kumar
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.12.032
Subject(s) - repressor , dna , förster resonance energy transfer , biophysics , operator (biology) , biology , chemistry , microbiology and biotechnology , genetics , fluorescence , gene , physics , transcription factor , quantum mechanics
λ‐Repressor–operator sites interaction, particularly O R 1 and O R 2, is a key component of the λ‐genetic switch. FRET from the dansyl bound to the C‐terminal domain of the protein, to the intercalated EtBr in the operator DNA indicates that the structure of the protein is more compact in the O R 2 complex than in the O R 1 complex. Fluorescence anisotropy reveals enhanced flexibility of the C‐terminal domain of the repressor at fast timescales after complex formation with O R 1. In contrast, O R 2 bound repressor shows no significant enhancement of protein dynamics at these timescales. These differences are shown to be important for correct protein–protein interactions. Altered protein dynamics upon specific DNA sequence recognition may play important roles in assembly of regulatory proteins at the correct positions.