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RPA, best known for its role in DNA replication and repair, recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation.
Single point mutations in the RPA32 subunit of RPA that abolish interaction with RFWD3 also inhibit interstrand crossling repair, demonstrating that RPA-mediated RFWD3 recruitment to stalled replication forks is important for ICL repair.
E3 ligase RFWD3 functions in timely removal and degradation of RPA and RAD51 to allow homologous recombination progression to subsequent steps following mitomycin C damage.
knockdown of RPA2 promoted formation of the menin-p65 complex and repressed the expression of NF-kappaB-mediated genes. RPA2 expression was induced via an E2F1-dependent mechanism in MCF7 and MDA-MB-231 cells treated with NF-kappaB activators, TNF-alpha or lipopolysaccharide (LPS).
The authors show that Vpr can form a trimolecular complex with UNG2 and RPA32 and the positive effect of UNG2 and RPA32 on the reverse transcription process leading to optimal virus replication and dissemination between the primary target cells of HIV-1.
RPA32 phosphorylation regulates replication arrest, recombination, late origin firing, and mitotic catastrophe
Expression of mutant RPA2 or loss of PALB2 expression led to significant DNA damage after replication stress, a defect accentuated by poly-ADP (adenosine diphosphate) ribose polymerase inhibitors.
Conserved motifs are required for RPA32 binding the the N-terminus of SMARCAL1.
study reports the characterization of the RPA32C-SMARCAL1 interface at the molecular level; implications of results are discussed with respect to the recruitment of SMARCAL1 and other DNA damage response and repair proteins to stalled replication forks
study concludes RPA2 expression is translationally regulated via internal ribosome entry site and by eIF3a and that this regulation is partly accountable for cellular response to DNA damage and survival.
this study has explored the role of RPA32 phosphorylation at CDK and ATR sites and propose that phosphorylation of the RPA32 subunit is dispensable for checkpoint activation induced by replication stress with aphidicolin.
4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2
Data show that the R88C variant impairs binding of the R88C variant impairs binding of uracil-DNA glycosylase UNG2 to replication protein A RPA2.
Replication protein A1, replication protein A2, and cyclins D2 and D3 seem to have a parallel role in the promotion of cell cycle in astrocytic tumors being implicated in the malignant progression of these neoplasms.
RPA1 and RPA2 overexpression seems to be more important during early T-categories of bladder carcinogenesis, showing similar kinetics with cyclin D1
RPA2 hyperphosphorylation by DNA-PK in response to DNA double-strand breaks blocks unscheduled homologous recombination and delays mitotic entry.
RPA2 up-regulation may be involved in the growth and/or survival of BRCA1 tumor cells and useful in immunohistochemical discrimination of triple-negative BRCA1 tumors.
At the subunit level, 13 proteins out of 30 examined may interact with RPA2.
data suggest that RPA2 hyperphosphorylation plays a critical role in maintenance of genomic stability and cell survival after a DNA replication block via promotion of homologus recombination
Data suggest that PP4-mediated dephosphorylation of RPA2 is necessary for an efficient DNA-damage response.
Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage (By similarity). Required for simian virus 40 DNA replication in vitro. It participates in a very early step in initiation.
RF-A protein 2
, RP-A p32
, RP-A p34
, replication factor A protein 2
, replication protein A 32 kDa subunit
, replication protein A 34 kDa subunit
, replication protein A, subunit 2
, replication protein A2
, p32-subunit of replication protein A
, RPA p32
, replication protein A2, 32kDa
, putative replication protein A middle subunit
, 30-kDa protein