Telomeres are nucleoprotein structures at the end of eukaryotic
chromosomes containing linear DNA. The telomere´s main function
is to protect chromosome ends from their degradation, fusion
and unwanted recognition by reparation mechanism of cells. The
telomere protection is mediated by telomeric proteins,
especially by proteins of shelterin complex. Shelterin complex
takes part in regulation of telomere length. It is important
because during each DNA replication telomeres shorten. The
enzyme called telomerase extends telomeres by adding of
nucleotides to their ends. Telomerase is active in most tumors.
Telomerase activity serves as a marker for diagnoses of cancer
transformation of tissues. Shelterin proteins regulate
telomerase access to telomeric DNA by creating T-loops.
Controlled reduction of telomerase activity mediated by
shelterin proteins can help to stop tumor growth.
This study is focused on interactions of shelterin proteins
TRF1 and TRF2 with telomeric DNA. The electrophoretic mobility
shift assay was used for a description of stechiometry of
interactions. Quantitative characterizations of binding
constants were carried out by using fluorescence anisotropy
measurements. The obtained results may contribute to a better
understanding of functions of shelterin complex proteins and
their contributions to the regulation of telomere length. This
could be employed in designing of new approaches to cancer
treatment.