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DNA polymerase beta -mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis.
TLDR
The DNA synthesis and flap excision steps in long patch BER are examined using a reconstituted system containing a 34-base pair BER substrate and five purified human enzymes: uracil-DNA glycosylase, apurinic/apyrimidinic endonuclease, DNA polymerase beta, flap end onuclease-1 (FEN-1), and PARP-1.
HMGB1 is a cofactor in mammalian base excision repair.
Apurinic/apyrimidinic (AP) site recognition by the 5′-dRP/AP lyase in poly(ADP-ribose) polymerase-1 (PARP-1)
TLDR
By virtue of its binding to AP sites, PARP-1 could be poised for its role in base excision repair, pending DNA strand incision by APE1 or the 5′-dRP/AP lyase activity in PARP -1.
Human replication protein A unfolds telomeric G-quadruplexes
TLDR
It is shown that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence, pointing to the involvement of hRPA in regulation of telomere maintenance.
Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase β and poly(ADP-ribose) polymerase 1: interplay between strand-displacement DNA synthesis and proofreading
TLDR
Differences in the stoichiometry of BER enzymes may regulate BER, as shown in the results of conditions of enzyme excess over substrate DNA.
Dna is a New Target of Parp3
TLDR
It is demonstrated that DNA-dependent PARP3 can modify DNA and form a specific primed structure for further use by the repair proteins and suggested that this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts.
Photoaffinity Labeling of Mouse Fibroblast Enzymes by a Base Excision Repair Intermediate
TLDR
It is shown that proteins interacting preferentially with a photoreactive BER intermediate can be selected from the crude cellular extract and the specificity of PARP-1 labeling was stronger with a DNA representing a B ER intermediate than with a nick in double-stranded DNA.
Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation
TLDR
It is shown that mammalian PARP2 and PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5′- and 3′-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks.
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