De, Amitabha and Ramesh, V and Mahadevan, S and Nagaraja, V (1998) Mg2+ Mediated Sequence-Specific Binding of Transcriptional Activator Protein C of Bacteriophage Mu to DNA. In: Biochemistry, 37 (11). pp. 3831-3838.
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The contributions from the secondary structure of the transcriptional activator protein C of bacteriophage Mu to its specific DNA binding and the influence of various factors, viz ., electrolytes, and minor groove and major groove binders on this protein-DNA interaction have been addressed . Circular dichroism (CD) spectral results suggest that, in the absence of Mg2+, C protein exhibits a j3-pleated sheetlike structure and Mg2+ changes the conformation to a more a-helical structure which could provide specific geometrical constraints complementary to those of DNA helix. Thus, Mg 2+ acts as a cofactor for the binding of the C protein to its specific site in DNA by inducing conformational changes in the protein. Competitive binding studies with minor and major groove binding drugs, viz ., distamycin A and methyl green, respectively, and the DMS footprinting data indicate that the C protein recognizes the major groove of DNA during complex formation . Further, upon major groove binding, C protein brings about changes in DNA conformation; such conformational changes could have implications in the transcription process.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to American Chemical Society.|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||08 Dec 2004|
|Last Modified:||19 Sep 2010 04:17|
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