Title of article :
Novel DNA–peptide interaction networks Original Research Article
Author/Authors :
Jonathan T.B. Huang، نويسنده , , Yen-Chung Chen، نويسنده , , Jung-Cheng Chang، نويسنده , , Kee-Ching G. Jeng، نويسنده , , Karen K.L. Kao، نويسنده , , Robin C.K. Yang، نويسنده , , Lou-Sing Kan، نويسنده , , Ming-Tsair Wey، نويسنده , , Michael J. Waring، نويسنده , , Chee-Shan Chen، نويسنده , , Wei-Jyun Chien، نويسنده , , Leung Sheh، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2010
Pages :
11
From page :
2575
To page :
2585
Abstract :
Allostery in the binding of peptides to DNA has been studied by quantitative DNase I footprinting using four newly designed peptides containing the XP(Hyp)RK motif and N-methylpyrrole (Py) moieties. Apparent binding constants in the micromolar range as well as Hill coefficients were determined for each peptide. The results, together with previous studies on five other peptides support the proposal that interaction network cooperativity is highly preferred in DNA–peptide interactions that involve multiple recognition sites. It is envisaged that interstrand bidentate interactions participate in the relay of conformational changes between recognition sites on the complementary strands. Models for interpreting DNA allostery based upon interaction networks are outlined. Circular dichroism experiments involving the titration of peptides against a short oligonucleotide duplex indicate that some of these peptides bind in a dimeric manner to DNA via the minor groove, inducing characteristic conformational changes. These insights should prompt the design of new DNA-binding peptides for investigating allosteric interactions between peptides and DNA, as well as novel interaction networks, and ultimately may shed light upon the fundamental chemical rules that govern allostery in more complex biological process such as DNA–protein interaction networks.
Keywords :
DNA–peptide molecular recognition , Footprinting , Positive cooperative binding , circular dichroism , Interaction networks
Journal title :
Bioorganic and Medicinal Chemistry
Serial Year :
2010
Journal title :
Bioorganic and Medicinal Chemistry
Record number :
1307261
Link To Document :
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