ArticleThe Journal of biological chemistry2009
Human replication factor C stimulates flap endonuclease 1.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- HNRNPLL stabilizes mRNA for DNA replication proteins and promotes cell cycle progression in colorectal cancer cells.Cancer science · 2018Article
- Role of PCNA and RFC in promoting Mus81-complex activity.BMC biology · 2017Article
- Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains.Nucleic acids research · 2017Article
- Sulfolobus replication factor C stimulates the activity of DNA polymerase B1.Journal of bacteriology · 2014Article
- Subcellular proteomics reveals a role for nucleo-cytoplasmic trafficking at the DNA replication origin activation checkpoint.Journal of proteome research · 2013Article
- Human Fanconi anemia complementation group a protein stimulates the 5' flap endonuclease activity of FEN1.PloS one · 2013Article
- The trans-autostimulatory activity of Rad27 suppresses dna2 defects in Okazaki fragment processing.The Journal of biological chemistry · 2012Article
- The DNA replication factor RFC1 is required for interference-sensitive meiotic crossovers in Arabidopsis thaliana.PLoS genetics · 2012Article
- Reconstitution of eukaryotic lagging strand DNA replication.Methods (San Diego, Calif.) · 2010Review
- Involvement of Vts1, a structure-specific RNA-binding protein, in Okazaki fragment processing in yeast.Nucleic acids research · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flap endonuclease 1 (FEN1) is the enzyme responsible for specifically removing the flap structure produced during DNA replication, repair, and recombination. Here we report that the human replication factor C (RFC) complex stimulates the nuclease activity of human FEN1 in an ATP-independent manner. Although proliferating cell nuclear antigen is also known to stimulate FEN1, less RFC was required for comparable FEN1 stimulation. Kinetic analyses indicate that the mechanism by which RFC stimulates FEN1 is distinct from that by proliferating cell nuclear antigen. Heat-denatured RFC or its subunit retained, fully or partially, the ability to stimulate FEN1. Via systematic deletion analyses, we have defined three specific regions of RFC4 capable of stimulating FEN1. The region of RFC4 with the highest activity spans amino acids 170-194 and contains RFC box VII. Four amino acid residues (i.e. Tyr-182, Glu-188, Pro-189, and Ser-192) are especially important for FEN1 stimulatory activity. Thus, RFC, via several stimulatory motifs per molecule, potently activates FEN1. This function makes RFC a critical partner with FEN1 for the processing of eukaryotic Okazaki fragments.
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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.