HPF1 Regulates Pol β Efficiency in Nucleosomes via the Modulation of Total Poly(ADP-Ribose) Synthesis DOI Open Access
Mikhail M. Kutuzov, Dinara Sayfullina, E. A. Belousova

и другие.

International Journal of Molecular Sciences, Год журнала: 2025, Номер 26(5), С. 1794 - 1794

Опубликована: Фев. 20, 2025

The maintenance of genome stability and the prevention genotoxic damage to DNA require immediate repair. In cell, repair process is usually preceded by a release from complexes with chromatin proteins accompanied nucleosome sliding, relaxing or disassembly. Base excision (BER) corrects most common lesions, which does not disturb helix dramatically. Notably, small lesions can be repaired in without global decompaction. One regulatory mechanisms poly(ADP-ribosyl)ation, leading relaxation nucleosome. our work, we demonstrated that recently discovered protein, HPF1, modulate efficiency one key BER stages-DNA synthesis-via regulation total poly(ADP-ribosyl)ation. Accordingly, investigated both short-patch long-patch synthesis catalyzed polymerase β (pol β; main BER) showed HPF1's influence on poly(ADP-ribosyl)ation PARP1 especially PARP2 results more efficient case pathway nucleosomes. Additionally, HPF1-dependent was found positively regulate BER.

Язык: Английский

Deciphering the dark side of histone ADP-ribosylation: what structural features of damaged nucleosome regulate the activities of PARP1 and PARP2 DOI Open Access
Tatyana A. Kurgina, Nina Moor, Mikhail M. Kutuzov

и другие.

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

Процитировано

0

HPF1 Regulates Pol β Efficiency in Nucleosomes via the Modulation of Total Poly(ADP-Ribose) Synthesis DOI Open Access
Mikhail M. Kutuzov, Dinara Sayfullina, E. A. Belousova

и другие.

International Journal of Molecular Sciences, Год журнала: 2025, Номер 26(5), С. 1794 - 1794

Опубликована: Фев. 20, 2025

The maintenance of genome stability and the prevention genotoxic damage to DNA require immediate repair. In cell, repair process is usually preceded by a release from complexes with chromatin proteins accompanied nucleosome sliding, relaxing or disassembly. Base excision (BER) corrects most common lesions, which does not disturb helix dramatically. Notably, small lesions can be repaired in without global decompaction. One regulatory mechanisms poly(ADP-ribosyl)ation, leading relaxation nucleosome. our work, we demonstrated that recently discovered protein, HPF1, modulate efficiency one key BER stages-DNA synthesis-via regulation total poly(ADP-ribosyl)ation. Accordingly, investigated both short-patch long-patch synthesis catalyzed polymerase β (pol β; main BER) showed HPF1's influence on poly(ADP-ribosyl)ation PARP1 especially PARP2 results more efficient case pathway nucleosomes. Additionally, HPF1-dependent was found positively regulate BER.

Язык: Английский

Процитировано

0