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Showing posts with the label Poly-(ADP-ribose) polymerases (PARPs)

Note for: PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes (2017)

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Note for: PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes (2017) doi: 10.1101/gad.291518.116 - Discovery of Poly(ADP-ribose) – more than 50 years - Only PARP1 has been extensively studied but not other PARPs - PARP1 has been studied in DNA damage detection and repair - Actually, PARPs have diverse range of biological roles (one of the PTMs) - Substrate for PARPs -- > protein or nucleicacid + NAD with ADP-ribose ADP-ribosylation - Reversible process which adding ADP-ribose from beta-NAD+ to protein – mono- or poly- - Catalyze the reaction called ADP-ribosylation reaction - This review focuses on o Mono(ADP-ribosylation) -- MARylation o Poly(ADP-ribosylation) -- PARylation o At amino acid site – glutamate, aspartate, and lysine residues PARPs - Writers of ADP-ribose Accessory proteins - Readers – contain ADP-ribose-binding domains (ARBD) Erasers - ADP-ribose and PAR hydrolases Feeders - Providing NAD+ (NAD+ s...

Note for: Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells

Note: Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells (doi: 10.1038/sj.emboj.7601015) Parp-1 and Parp-2 -- responsible for SSB repair but the role of these two in HR is not clear. Using DT40 as a tool to study. DT40 has only Parp-1, no Parp-2. Parp-1(-/-) reduced the level of HR, sensitive to various DSB-inducing genotoxic agents. More sensitive when having Ku which is the DSB-binding factor. PARP1+KU70 -- proficient in initiate HR and show resistance to DSB-inducing drugs. In conclusion - having parp-1 suppress the Ku70 function and NHEJ on HR. there are so many parps (poly (ADP-ribosylation) proteins -- in mammalian, it contains 17 parps, only parp1 and parp2 act on the DNA damage response. Prarp1 and 2 interact with each other and found in the large cpx with XRCC1 and DNA-pol-beta and DNA ligase III. Evident has showed Parp1 and parp2 play role in base excision repair (BER) on damage detection, signaling and...