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Nucleic Acids Research Advance Access published online on November 25, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn919
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Metastases suppressor NM23-H2 interaction with G-quadruplex DNA within c-MYC promoter nuclease hypersensitive element induces c-MYC expression

Ram Krishna Thakur1, Praveen Kumar1, Kangkan Halder1, Anjali Verma1, Anirban Kar1, Jean-Luc Parent2, Richa Basundra1, Akinchan Kumar1 and Shantanu Chowdhury1,3,*

1Proteomics and Structural Biology Unit, Institute of Genomics and Integrative Biology, CSIR, Delhi, India, 2Division of Rheumatology, Faculty of Medicine, University of Sherbrooke, Fleurimont, Quebec J1H 5N4, Canada and 3G. N. Ramachandran Knowledge Centre for Genome Informatics, Institute of Genomics and Integrative Biology, CSIR, Delhi, India

*To whom correspondence should be addressed. Tel: +91 11 2766 6157; Fax: +91 11 2766 7471; Email: shantanuc{at}igib.res.in

Received July 25, 2008. Revised October 29, 2008. Accepted November 2, 2008.

Regulatory influence of the G-quadruplex or G4 motif present within the nuclease hypersensitive element (NHE) in the promoter of c-MYC has been noted. On the other hand, association of NM23-H2 to the NHE leads to c-MYC activation. Therefore, NM23-H2 interaction with the G4 motif within the c-MYC NHE presents an interesting mechanistic possibility. Herein, using luciferase reporter assay and chromatin immunoprecipitation we show NM23-H2 mediated c-MYC activation involves NM23-H2-G4 motif binding within the c-MYC NHE. G4 motif complex formation with recombinant NM23-H2 was independently confirmed using fluorescence energy transfer, which also indicated that the G4 motif was resolved to an unfolded state within the protein-bound complex. Taken together, this supports transcriptional role of NM23-H2 via a G4 motif.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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