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Flap structure-specific endonuclease 1

rad2, FEN1, MF1, RAD27
The protein encoded by this gene removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5' end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: FLAP, CAN, POLYMERASE, HAD, ACID
Papers on rad2
TGF-β1 levels and intraocular tissue alterations in mice infected with a virulent type I RH Toxoplasma gondii strain.
Raghupathy et al., Kuwait, Kuwait. In Exp Parasitol, Feb 2016
In this study, we studied intraocular immune response and tissue alterations in the genetically resistant BALB/c and susceptible MF1 mice infected with a virulent type I RH T. gondii strain by intravitreal route.
Flap endonuclease 1 silencing is associated with increasing the cisplatin sensitivity of SGC‑7901 gastric cancer cells.
Chen et al., Chongqing, China. In Mol Med Report, Jan 2016
Flap endonuclease 1 (FEN1), which is key in DNA replication and repair, has been demonstrated to be intimately involved in the development and progression of cancer.
Wuho Is a New Member in Maintaining Genome Stability through its Interaction with Flap Endonuclease 1.
Hsieh et al., Taipei, Taiwan. In Plos Biol, Jan 2016
We identify that the flap endonuclease 1 (FEN1) is one of the interacting proteins.
Shade avoidance 6 encodes an Arabidopsis flap endonuclease required for maintenance of genome integrity and development.
Tao et al., Xiamen, China. In Nucleic Acids Res, Jan 2016
UNASSIGNED: Flap endonuclease-1 (FEN1) belongs to the Rad2 family of structure-specific nucleases.
RECQL5 has unique strand annealing properties relative to the other human RecQ helicase proteins.
Bohr et al., Baltimore, United States. In Dna Repair (amst), Jan 2016
Additionally, we investigate how different known RecQ interacting proteins, RPA, Ku, FEN1 and RAD51, regulate their strand annealing activity.
Primer removal during mammalian mitochondrial DNA replication.
Falkenberg et al., Göteborg, Sweden. In Dna Repair (amst), Oct 2015
The nucleases RNase H1, FEN1, DNA2, and MGME1 have been implicated in this process.
Recognition and repair of chemically heterogeneous structures at DNA ends.
Williams et al., United States. In Environ Mol Mutagen, 2015
Nucleolytic processing enzymes such as the MRE11/RAD50/NBS1/CtIP complex, Flap endonuclease (FEN1) and the apurinic endonucleases (APE1 and APE2) also act in the chemical "cleansing" of DNA breaks to prevent genomic instability and disease, and promote progression of DNA- and RNA-DNA damage response (DDR and RDDR) pathways.
The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once.
Tainer et al., Berkeley, United States. In Dna Repair (amst), 2014
Here, we review protein-DNA structures for nucleases involved in replication, base excision repair, mismatch repair, double strand break repair (DSBR), and telomere maintenance: apurinic/apyrimidinic endonuclease 1 (APE1), Endonuclease IV (Nfo), tyrosyl DNA phosphodiesterase (TDP2), UV Damage endonuclease (UVDE), very short patch repair endonuclease (Vsr), Endonuclease V (Nfi), Flap endonuclease 1 (FEN1), exonuclease 1 (Exo1), RNase T and Meiotic recombination 11 (Mre11).
Large-scale genetic study in East Asians identifies six new loci associated with colorectal cancer risk.
Zheng et al., Nashville, United States. In Nat Genet, 2014
Four other loci are located in or near genes involved in transcriptional regulation (ZMIZ1), genome maintenance (FEN1), fatty acid metabolism (FADS1 and FADS2), cancer cell motility and metastasis (CD9), and cell growth and differentiation (NXN).
Poxvirus DNA replication.
Moss, Bethesda, United States. In Cold Spring Harb Perspect Biol, 2013
A viral FEN1 family protein participates in double-strand break repair.
My journey to DNA repair.
Lindahl, London, United Kingdom. In Genomics Proteomics Bioinformatics, 2013
I discovered the mammalian exonucleases DNase III (TREX1) and IV (FEN1).
Flap endonuclease 1.
Bambara et al., Rochester, United States. In Annu Rev Biochem, 2012
First discovered as a structure-specific endonuclease that evolved to cut at the base of single-stranded flaps, flap endonuclease (FEN1) is now recognized as a central component of cellular DNA metabolism.
Sequential posttranslational modifications program FEN1 degradation during cell-cycle progression.
Shen et al., Nanjing, China. In Mol Cell, 2012
Cell-cycle-dependent timing of FEN1 nuclease activity is essential for cell-cycle progression and the maintenance of genome stability.
Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2.
Omichinski et al., Montréal, Canada. In Nucleic Acids Res, 2012
Structure determination of a Rad2-Tfb1PH complex indicates that Rad2 binds to TFIIH using a similar motif as TFIIEalpha uses to bind TFIIH in the pre-initiation complex.
Structural basis of nuclear import of flap endonuclease 1 (FEN1).
Fontes et al., Botucatu, Brazil. In Acta Crystallogr D Biol Crystallogr, 2012
The crystal structure of the complex of importin alpha with a peptide corresponding to the FEN1 nuclear localization sequence was solved.
Adenomatous polyposis coli interacts with flap endonuclease 1 to block its nuclear entry and function.
Narayan et al., Gainesville, United States. In Neoplasia, 2012
These studies demonstrate a novel role for APC in the suppression of Fen1 activity in the BER pathway
Repair complexes of FEN1 endonuclease, DNA, and Rad9-Hus1-Rad1 are distinguished from their PCNA counterparts by functionally important stability.
Ivanov et al., Berkeley, United States. In Proc Natl Acad Sci U S A, 2012
Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies.
Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.
Beese et al., Durham, United States. In Cell, 2011
It is a member of the 5' structure-specific nuclease family of exonucleases and endonucleases that includes FEN-1, XPG, and GEN1.
FEN nucleases: bind, bend, fray, cut.
Kunkel et al., United States. In Cell, 2011
In this issue, Orans et al. (2011) and Tsutakawa et al. (2011) report exciting insights into the molecular principles governing diverse endo- and exonucleolytic cleavage specificities of members of the RAD2/FEN superfamily of nucleases, which have critical roles in DNA replication and maintenance.
Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily.
Tainer et al., Berkeley, United States. In Cell, 2011
Structural and functional analyses of human FEN1:DNA complexes show structure-specific, sequence-independent recognition for nicked dsDNA bent 100 degrees with unpaired 3' and 5' flaps.
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