Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1

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Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1. / Kurgina, T. A.; Lavrik, O. I.

In: Molecular Biology, Vol. 57, No. 2, 04.2023, p. 245-257.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{ea77918a2f0b4241bf11dfd47fc6c8a0,

title = "Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1",

abstract = "Poly(ADP-ribose) (PAR) is a negatively charged polymer, linear or branched, that consists of ADP-ribose monomers. PAR is synthesized by poly(ADP-ribose)polymerase (PARP) enzymes, which are activated upon DNA damage and use nicotinamide adenine dinucleotide (NAD+) as a substrate. The best-studied members of the PARP family, PARP1 and PARP2, are the most important nuclear proteins involved in many cell processes, including the regulation of DNA repair. PARP1 and PARP2 catalyze PAR synthesis and transfer to amino acid residues of target proteins, including autoPARylation. PARP1 and PARP2 are promising targets for chemotherapy in view of their key role in regulating DNA repair. A novel histone PARylation factor (HPF1) was recently discovered to modulate PARP1/2 activity by forming a transient joint active site with PARP1/2. Histones are modified at serine residues in the presence of HPF1. The general mechanism of the interaction between HPF1 and PARP1/2 is a subject of intense research now. The review considers the discovery and classical mechanism of PARylation in higher eukaryotes and the role of HPF1 in the process.",

keywords = "HPF1, PARP1, PARP2, PARylation, histones, poly(ADP-ribose), poly(ADP-ribosyl)ation",

author = "Kurgina, {T. A.} and Lavrik, {O. I.}",

note = "This work was supported by the Russian Science Foundation (project no. 22-14-00112) and a state contract with the Institute of Chemical Biology and Fundamental Medicine (no. 121031300041-4, part “Several Aspects of the Roles of PARP1 and PARP2 in the Cell”). Публикация для корректировки.",

year = "2023",

month = apr,

doi = "10.1134/S0026893323020140",

language = "English",

volume = "57",

pages = "245--257",

journal = "Molecular Biology",

issn = "0026-8933",

publisher = "Maik Nauka-Interperiodica Publishing",

number = "2",

}

RIS

TY - JOUR

T1 - Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1

AU - Kurgina, T. A.

AU - Lavrik, O. I.

N1 - This work was supported by the Russian Science Foundation (project no. 22-14-00112) and a state contract with the Institute of Chemical Biology and Fundamental Medicine (no. 121031300041-4, part “Several Aspects of the Roles of PARP1 and PARP2 in the Cell”). Публикация для корректировки.

PY - 2023/4

Y1 - 2023/4

N2 - Poly(ADP-ribose) (PAR) is a negatively charged polymer, linear or branched, that consists of ADP-ribose monomers. PAR is synthesized by poly(ADP-ribose)polymerase (PARP) enzymes, which are activated upon DNA damage and use nicotinamide adenine dinucleotide (NAD+) as a substrate. The best-studied members of the PARP family, PARP1 and PARP2, are the most important nuclear proteins involved in many cell processes, including the regulation of DNA repair. PARP1 and PARP2 catalyze PAR synthesis and transfer to amino acid residues of target proteins, including autoPARylation. PARP1 and PARP2 are promising targets for chemotherapy in view of their key role in regulating DNA repair. A novel histone PARylation factor (HPF1) was recently discovered to modulate PARP1/2 activity by forming a transient joint active site with PARP1/2. Histones are modified at serine residues in the presence of HPF1. The general mechanism of the interaction between HPF1 and PARP1/2 is a subject of intense research now. The review considers the discovery and classical mechanism of PARylation in higher eukaryotes and the role of HPF1 in the process.

AB - Poly(ADP-ribose) (PAR) is a negatively charged polymer, linear or branched, that consists of ADP-ribose monomers. PAR is synthesized by poly(ADP-ribose)polymerase (PARP) enzymes, which are activated upon DNA damage and use nicotinamide adenine dinucleotide (NAD+) as a substrate. The best-studied members of the PARP family, PARP1 and PARP2, are the most important nuclear proteins involved in many cell processes, including the regulation of DNA repair. PARP1 and PARP2 catalyze PAR synthesis and transfer to amino acid residues of target proteins, including autoPARylation. PARP1 and PARP2 are promising targets for chemotherapy in view of their key role in regulating DNA repair. A novel histone PARylation factor (HPF1) was recently discovered to modulate PARP1/2 activity by forming a transient joint active site with PARP1/2. Histones are modified at serine residues in the presence of HPF1. The general mechanism of the interaction between HPF1 and PARP1/2 is a subject of intense research now. The review considers the discovery and classical mechanism of PARylation in higher eukaryotes and the role of HPF1 in the process.

KW - HPF1

KW - PARP1

KW - PARP2

KW - PARylation

KW - histones

KW - poly(ADP-ribose)

KW - poly(ADP-ribosyl)ation

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85156109917&origin=inward&txGid=71e3958bc46a53bd1aea35cad24d969a

UR - https://www.mendeley.com/catalogue/f4e83d52-ab32-3621-a49e-2d164c7e77e6/

U2 - 10.1134/S0026893323020140

DO - 10.1134/S0026893323020140

M3 - Article

VL - 57

SP - 245

EP - 257

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 59649421