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Mode of DNA binding with gamma-butyrolactone receptor protein CprB from Streptomyces coelicolor revealed by site-specific fluorescence dynamics

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Title Mode of DNA binding with gamma-butyrolactone receptor protein CprB from Streptomyces coelicolor revealed by site-specific fluorescence dynamics
 
Creator BISWAS, A
NARAYAN, S
KALLIANPUR, MV
KRISHNAMOORTHY, G
ANAND, R
 
Subject TIME-RESOLVED FLUORESCENCE
EUKARYOTIC TRANSCRIPTION FACTORS
MAXIMUM-ENTROPY METHOD
AUTOREGULATOR-RECEPTOR
2-AMINOPURINE FLUORESCENCE
ANTIBIOTIC PRODUCTION
SIGNALING MOLECULES
TETR FAMILY
A3(2)
RECOGNITION
2-Aminopurine
gamma-Butyrolactone
Anisotropy
Fluorescence lifetime
 
Description Background: The gamma-butyrolactone (GBL) binding transcription factors in Streptomyces species are known for their involvement in quorum sensing where they control the expression of various genes initiating secondary metabolic pathways. The structurally characterized member of this family CprB from Streptomyces coelicolor had earlier been demonstrated to bind a multitude of sequences containing a specific binding signature. Though structural breakthrough has been obtained for its complex with a consensus DNA sequence there is, however a dearth of information regarding the overall and site specific dynamics of protein-DNA interaction. Methods: To delineate the effect of CprB on the bound DNA, changes in motional dynamics of the fluorescent probe 2-aminopurine were monitored at three conserved base positions (5th, 12th and 23rd) for two DNA sequences: the consensus and the biologically relevant cognate element, on complex formation. Results: The changes in lifetime and generalized order parameter revealed a similarity in the binding pattern of the protein to both sequences with greater dynamic restriction at the end positions, 5th and 23rd, as compared to the middle 12th position. Also differences within this pattern demonstrated the influence of even small changes in sequence on protein interactions. Conclusions: Here the study of motional dynamics was instrumental in establishing a structural footprint for the cognate DNA sequence and explaining the dynamics for the consensus DNA from structural correspondence. General significance: Motional dynamics can be a powerful tool to efficiently study the mode of DNA binding to proteins that interact differentially with a plethora of DNA sequences, even in the absence of structural breakthrough. (C) 2015 Elsevier B.V. All rights reserved.
 
Publisher ELSEVIER SCIENCE BV
 
Date 2016-01-14T13:03:50Z
2016-01-14T13:03:50Z
2015
 
Type Article
 
Identifier BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1850(11)2283-2292
0304-4165
1872-8006
http://dx.doi.org/10.1016/j.bbagen.2015.08.008
http://dspace.library.iitb.ac.in/jspui/handle/100/17567
 
Language en