Polarized ultraviolet resonance Raman scattering at 266 nm was used to investigate the interaction of BRACO-19 and Pyridostatin with G-quadruplexes having different structural conformations.

Nucleic acids can fold into G-quadruplex (G4) structures that can fine-tune biological processes. Proteins are required to recognize G4 structures and coordinate their function. Here we identify Zuo1 as a novel G4-binding protein in vitro and in vivo. In vivo in the absence of Zuo1 fewer G4 structures form, cell growth slows and cells become UV sensitive. Subsequent experiments reveal that these cellular changes are due to reduced levels of G4 structures. Zuo1 function at G4 structures results in the recruitment of nucleotide excision repair (NER) factors, which has a positive effect on genome stability. Cells lacking functional NER, as well as Zuo1, accumulate G4 structures, which become accessible to translesion synthesis. Our results suggest a model in which Zuo1 supports NER function and regulates the choice of the DNA repair pathway nearby G4 structures.

Mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography have been used to investigate the reaction of CO-releasing molecule Cs₂IrCl₅CO with the model protein RNase A.

The G-quadruplex-forming telomeric sequence (TTAGGG) ₄ TT was investigated by polarized Ultraviolet Resonance Raman Scattering (UVRR) at 266 nm.