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Nucleic Acids Research, 2001, Vol. 29, No. 16 3377-3384
© 2001 Oxford University Press

N{omega}-arginine dimethylation modulates the interaction between a Gly/Arg-rich peptide from human nucleolin and nucleic acids

Baktisaran Raman, Corrado Guarnaccia, Katalin Nadassy1, Sotir Zakhariev, Alessandro Pintar, Francesco Zanuttin, Dávid Frigyes, Cristina Acatrinei, Alessandro Vindigni, Gábor Pongor2 and Sándor Pongor*

International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste, Italy, 1EMBL Outstation, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK and Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, UK and 2Department of Theoretical Chemistry, Eötvös Loránd University, PO Box 32, H-1518 Budapest 112, Hungary

We studied the interaction between a synthetic peptide (sequence Ac-GXGGFGGXGGFXGGXGG-NH2, where X = arginine, N{omega},N{omega}-dimethylarginine, DMA, or lysine) corresponding to residues 676–692 of human nucleolin and several DNA and RNA substrates using double filter binding, melting curve analysis and circular dichroism spectroscopy. We found that despite the reduced capability of DMA in forming hydrogen bonds, N{omega},N{omega}-dimethylation does not affect the strength of the binding to nucleic acids nor does it have any effect on stabilization of a double-stranded DNA substrate. However, circular dichroism studies show that unmethylated peptide can perturb the helical structure, especially in RNA, to a much larger extent than the DMA peptide.

* To whom correspondence should be addressed. Tel: +39 040 375 7300; Fax: +39 040 226 555; Email: pongor{at}icgeb.trieste.it


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