LncRNAs and the Cancer Epigenome: Mechanisms and Therapeutic Potential

Cancer Letters, Год журнала: 2024, Номер 605, С. 217297 - 217297

Опубликована: Окт. 16, 2024

Язык: Английский

Deciphering the dark side of histone ADP-ribosylation: what structural features of damaged nucleosome regulate the activities of PARP1 and PARP2

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2025, Номер unknown

Опубликована: Янв. 30, 2025

ABSTRACT Poly(ADP-ribose) polymerases are critical enzymes contributing to regulation of numerous cellular processes, including DNA repair. Within the PARP family, PARP1 and PARP2 primarily facilitate PARylation in nucleus, particularly responding genotoxic stress. The activity PARPs is influenced by nature damage multiple protein partners, with HPF1 being important one. Forming a joint active site (PARP2), contributes histone following chromatin remodelling during stress events. This study elucidates interrelation between presence location one-nucleotide gap within nucleosome core particle (NCP) activities automodification heteromodification histones. Utilizing combination classical biochemical methods fluorescence-based technique single-molecule mass photometry approach, we have shown that NCP architecture impacts efficiency pattern ADP-ribosylation binding histones-associated damaged more significantly for than PARP1. Analysis based on existing studies HPF1-dependent ADP-ribosylome structural dynamics allows suggest conformational flexibility tails modulated post-translational modifications crucial delineating distinct roles responses. GRAPHICAL

Язык: Английский

Histone modification inhibitors: An emerging frontier in thyroid Cancer therapy

Cellular Signalling, Год журнала: 2025, Номер unknown, С. 111703 - 111703

Опубликована: Март 1, 2025

Язык: Английский