Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives

Emanuela Micheli (1, 2) , Matteo Martufi (1) , Stefano Cacchione (1) , Pasquale de Santis (2) , Maria Savino (1)

1 Dipartimento di Biologia e Biotecnologie
2 Dipartimento di Chimica [Roma]

hTERT core promoter regulates telomerase transcription in human cells, thus its structural features are of large interest. We have found that the G-rich hTERT core promoter region, corresponding to the major DNase I hypersensitive site in chromatin organization, contains nine putative G-quadruplex forming sequences (PQS) and is unfavourable for nucleosome formation. Here we show that four PQS are effectively able to form stable parallel intramolecular G-quadruplexes, using PAGE and CD spectroscopy analysis. The PQS-region, as whole, appears to be organized in three self-interacting G-quadruplexes, probably giving rise to a helicoidal superstructure, as shown by CD and polymerase stop assay.

Mots clés: G-quadruplex; Telomerase; hTERT promoter; Perylene derivatives; Induced circular dichroism (ICD)

Domaines: Chimie-Physique [physics.chem-ph]

Emanuela Micheli, Matteo Martufi, Stefano Cacchione, Pasquale de Santis, Maria Savino. Self-organization of G-quadruplex structures in the hTERT core promoter stabilized by polyaminic side-chains perylene derivatives. Biophysical Chemistry, 2010, 153 (1), pp.43. ⟨10.1016/j.bpc.2010.10.003⟩. ⟨hal-00702310⟩