ArticleMolecular and cellular biology1997
Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNA.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Multiple biochemical properties of the p53 molecule contribute to activation of polymerase iota-dependent DNA damage tolerance.Nucleic acids research · 2020Article
- Dynamic elements of replication protein A at the crossroads of DNA replication, recombination, and repair.Critical reviews in biochemistry and molecular biology · 2020Review
- Replication protein A dynamically regulates monoubiquitination of proliferating cell nuclear antigen.The Journal of biological chemistry · 2019Article
- DNA-PK, ATM and ATR collaboratively regulate p53-RPA interaction to facilitate homologous recombination DNA repair.Oncogene · 2013Article
- A small molecule directly inhibits the p53 transactivation domain from binding to replication protein A.Nucleic acids research · 2013Article
- Replication-mediated disassociation of replication protein A-XPA complex upon DNA damage: implications for RPA handing off.Cell biology international · 2012Article
- A flexible linker region in Fip1 is needed for efficient mRNA polyadenylation.RNA (New York, N.Y.) · 2011Article
- Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modes.Biochemistry · 2006Article
- Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain.Nucleic acids research · 2005Article
- Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA.Journal of virology · 2004Article
- Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes.The EMBO journal · 2003Article
- The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene.Molecular and cellular biology · 2003Article
- Autoimmunity to the M(r) 32,000 subunit of replication protein A in breast cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2002Article
- The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding.Nucleic acids research · 2001Article
- UV-induced hyperphosphorylation of replication protein a depends on DNA replication and expression of ATM protein.Molecular biology of the cell · 2001Article
- Article
- Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.The EMBO journal · 2001Article
- Molecular interaction map of the mammalian cell cycle control and DNA repair systems.Molecular biology of the cell · 1999Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human replication protein A (RP-A) (also known as human single-stranded DNA binding protein, or HSSB) is a multisubunit complex involved in both DNA replication and repair. Potentially important to both these functions, it is also capable of complex formation with the tumor suppressor protein p53. Here we show that although p53 is unable to prevent RP-A from associating with a range of single-stranded DNAs in solution, RP-A is able to strongly inhibit p53 from functioning as a sequence-specific DNA binding protein when the two proteins are complexed. This inhibition, in turn, can be regulated by the presence of various lengths of single-stranded DNAs, as RP-A, when bound to these single-stranded DNAs, is unable to interact with p53. Interestingly, the lengths of single-stranded DNA capable of relieving complex formation between the two proteins represent forms that might be introduced through repair and replicative events. Increasing p53 concentrations can also overcome the inhibition by steady-state levels of RP-A, potentially mimicking cellular points of balance. Finally, it has been shown previously that p53 can itself be stimulated for site-specific DNA binding when complexed through the C terminus with short single strands of DNA, and here we show that p53 stays bound to these short strands even after binding a physiologically relevant site. These results identify a potential dual role for single-stranded DNA in the regulation of DNA binding by p53 and give insights into the p53 response to DNA damage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.