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2 Polish Journal of Chemistry

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The Application of Qualitative Analysis of DNA Bulky Adducts in the Diagnoosis of Brain Tumours

Barciszewska A., Gawrońska I., Żukiel R., Nowak S., Barciszewska M. Z.

Polish Journal of Chemistry

2003

Vol. 77 / nr 11

1607-1614

Damage to DNA(base modification) is generally considered to be causative and directly related to tumour formation. Interaction of chemical carcinogens with DNA either directly or after metabolic activation, typically involves covalent binding of an electrophilic compound with a nucleophilic site in DNA. Guanine is by far the most prevalent target although adducts have been reported for all bases. We analysed the occurrence of bulky hydrophobic derivatives of DNA (adducts) in human brain tumour tissues. DNA was isolated, enzymatically digested to nucleotides and labeled with [_-32P]ATP and T4 polynucleotide kinase. Radioactive nucleotides were separated on anion-exchange polyethyleneimine cellulose (PEI) thin layer chromatography (TLC).We found that all brain tumours have similar DNA adducts pattern, although there are some significant differences for a particular disease. It turned out that DNA of a glioblastoma multiforme contains a rich array of modified bases in contrast to meningeoma tissues DNA, which shows only a few nucleotides. Location of spots on TLC of DNA adducts resemble a triangle, which is specific for brain tumours. This method of analysis may be very useful in classification and clinical diagnosis of brain tumours.

Interaction of a Transcription Factor IIIA Peptide Containing Two Zinc Fingers with 5S rRNA

Giel-Pietraszuk M., Mucha P., Rekowski P., Kupryszewski G., Barciszewska M. Z.

Polish Journal of Chemistry

2002

Vol. 76 / nr 6

815-822

The interaction of lupin ribosomal 5S RNA with a chemically synthesized peptide containing 60 amino acid, derived from Xenopus laevis transcription factor IIIA, is analyzed. The results show that such short fragment retains the ability of binding to 5S rRNA molecule, as shown by electrophoretic gel shift and RNase footprint assay. The peptide protects from hydrolysis with specific nucleases helix II and V of 5S rRNA.