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DNA polymerase beta -mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis.
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)
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
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
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
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
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
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.