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loss-of-function alleles indicate that RPA is required to prevent neuroepithelial cells from differentiating into medulla neuroblasts
Data show that the basic cleft of the RPA70 N-terminal OB-fold domain binds multiple checkpoint proteins, including RAD9, to promote ATR signaling.
The authors establish that a second Dna2-Rpa interaction is mutually exclusive with Rpa-DNA interactions and mediates the displacement of Rpa from ssDNA.
LT prevents recruitment of RPA to nuclear foci after DNA damage. This leads to failure to recruit repair proteins such as Rad51 (show RAD51 ELISA Kits) or Rad9 (show RAD9A ELISA Kits), explaining why LT prevents repair of double strand DNA breaks by homologous recombination.
Most RPA recruitment during class switch recombination represents salvage of unrepaired breaks by homology-based pathways during the S-G2 (show STRN3 ELISA Kits)/M phase of the cell cycle.
POT1a (show POT1 ELISA Kits) degradation resulted in rapid and reversible activation of the ATR (show ATR ELISA Kits) pathway in G1 and S/G2 (show STRN3 ELISA Kits).
Rpa1(L230P) missense mutation significantly alters the tumor phenotype and spectrum of Trp53 (show TP53 ELISA Kits) mutant mice by modifying the genetic mechanisms underlying tumorigenesis.
both TNFR-p55 (show TNFRSF1A ELISA Kits) and TNFR (show TNFRSF1A ELISA Kits)-p75 (show NGFR ELISA Kits) appear to be of minimal importance for modulation of Fas (show FAS ELISA Kits)-mediated apoptosis and associated A1 protein expression despite normal Fas (show FAS ELISA Kits)/TNFR-p55 (show TNFRSF1A ELISA Kits) and increased TNFR (show TNFRSF1A ELISA Kits)-p75 (show NGFR ELISA Kits) expression in neutrophils
Rpa1 functions in DNA metabolism are essential for the maintenance of chromosomal stability and tumor suppression.
hyperphosphorylation may play a role in modulating cellular pathways by altering the DNA binding domain-mediated RPA-DNA and RPA-protein interactions, hypothetically via the interaction of hyperphosphorylated RPA32N with DBD-B
These results demonstrate that neither RPA hyper-phosphorylation nor H2AX are required for the formation in RPA intra-nuclear foci in response to DNA damage/replicational stress.
The results suggest that RPA phosphorylation enhances the recruitment of PRP19 to RPA-ssDNA and stimulates RPA ubiquitylation through a process requiring both PRP19 and RFWD3, thereby triggering a phosphorylation-ubiquitylation circuitry that promotes ATR activation and homologous recombination.
RPA recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation.
RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability.
Annealing helicase HARP closes RPA-stabilized DNA bubbles non-processively.
Architectural plasticity of human BRCA2 (show BRCA2 ELISA Kits)-RPA-RAD51 (show RAD51 ELISA Kits) complexes in DNA break repair has been described.
Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex.
Data suggest RAD52 (show RAD52 ELISA Kits) binds tightly to RPA/ssDNA complex in presynaptic complex and inhibits RPA turnover; during presynaptic complex assembly, most of RPA and RAD52 (show RAD52 ELISA Kits) is displaced from ssDNA, but some RAD52 (show RAD52 ELISA Kits)/RPA/ssDNA complexes persist as interspersed clusters surrounded by RAD51 (show RAD51 ELISA Kits) filaments. (RAD52 (show RAD52 ELISA Kits) = Rad52 (show RAD52 ELISA Kits) DNA repair/recombination protein (show RAD50 ELISA Kits); RPA = replication protein A; ssDNA = single-stranded DNA; RAD51 (show RAD51 ELISA Kits) = Rad51 (show RAD51 ELISA Kits) recombinase (show RAG1 ELISA Kits))
Data suggest that, during human DNA replication, restricting PCNA (proliferating cell nuclear antigen (show PCNA ELISA Kits)) to the vicinity of its DNA target site is important; PCNA (show PCNA ELISA Kits) can be maintained at or near primer/template junctions during DNA synthesis by RPA (replication protein A) or SSB (single-stranded DNA-binding protein); here, the SSB used was from Escherichia coli.
Strikingly, the addition of the single-stranded DNA (ssDNA)-binding replication protein A (RPA) selectively restores XPF-ERCC1 endonuclease activity on this structure. The 5'-3' exonuclease SNM1A can load from the XPF-ERCC1-RPA-induced incisions and digest past the crosslink to quantitatively complete the unhooking reaction.
The authors have discovered a major sub-pathway of conventional long-patch base excision repair that involves formation of a 9-nucleotide gap 5' to the lesion. This new sub-pathway is mediated by RECQ1 (show RECQL ELISA Kits) DNA helicase and ERCC1 (show ERCC1 ELISA Kits)-XPF (show ERCC4 ELISA Kits) endonuclease in cooperation with PARP1 poly(ADP-ribose) polymerase (show PARP1 ELISA Kits) and RPA.
This study found that the N-terminus of the RPA large subunit interacts with both WRN and DNA2 (show DNA2 ELISA Kits) and is essential for stimulating WRN's 3'->5' helicase (show DNA2 ELISA Kits) activity and DNA2 (show DNA2 ELISA Kits)'s 5'->3' ss-DNA exonuclease (show EXO1 ELISA Kits) activity.
The results provide strong biochemical evidence to link RPA to a specific DSB repair pathway and reveal a novel function of RPA in the generation of 3' ss-DNA for homology-dependent DSB repair.
Replication protein A accumulated increasingly on replication-arrested chromatin.
RPA1 subunit may directly recognize and bind to the 5-formyluracil on the single-stranded DNA.
Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair\; it does not support chromosomal DNA replication and cell cycle progression through S- phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.
, drosophila replication protein A
, replication protein A 70
, single stranded-binding protein 70
, replication protein A1, 70kDa
, replication protein A 70 kDa DNA-binding subunit
, RF-A protein 1
, RP-A p70
, replication factor A protein 1
, replication protein A1
, replication protein A 70 kDa DNA-binding subunit-like
, single-stranded DNA-binding protein
, replication protein A (RPA)
, single-stranded DNA binding
, single-stranded DNA-binding protein, mitochondrial