Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300 (Q24291379)

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M Stucki

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P O Hassa

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R Imhof

4

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P Gehrig

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P Hunziker

6

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U Hübscher

7

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M O Hottiger

Characterization of the Enzymatic Properties of the Yeast Dna2 Helicase/Endonuclease Suggests a New Model for Okazaki Fragment Processing

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language of work or name

English

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publication date

June 2001

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published in

Molecular Cell

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volume

7

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page(s)

1221-31

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issue

6

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cites work

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A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function

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A human RNA polymerase II complex containing factors that modify chromatin structure

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Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor

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Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

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The characterization of a mammalian DNA structure-specific endonuclease

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Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: implications for nucleotide excision repair

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Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis

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Double-strand break repair in yeast requires both leading and lagging strand DNA polymerases

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Flap endonuclease homologs in archaebacteria exist as independent proteins.

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Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity

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The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

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Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen

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Proliferating cell nuclear antigen: more than a clamp for DNA polymerases

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HIV-1 tat transcriptional activity is regulated by acetylation

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Binding properties of replication protein A from human and yeast cells

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Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1).

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Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen

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The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair

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p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage

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Regulation of E2F1 activity by acetylation

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DNA polymerase switching: II. Replication factor C abrogates primer synthesis by DNA polymerase alpha at a critical length

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

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Characterization of a mutant strain of Saccharomyces cerevisiae with a deletion of the RAD27 gene, a structural homolog of the RAD2 nucleotide excision repair gene

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DNA damage activates p53 through a phosphorylation-acetylation cascade

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The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering 1 1Edited by M. F. Moody

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Cell cycle regulation of the transcriptional coactivators p300 and CREB binding protein

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Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5'- to 3'-exonuclease required for lagging strand DNA synthesis in reconstituted systems

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In eukaryotic flap endonuclease 1, the C terminus is essential for substrate binding

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Homologous recombination is required for the viability of rad27 mutants

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Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1

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Transcriptional activators direct histone acetyltransferase complexes to nucleosomes

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Mutations in RAD27 define a potential link between G1 cyclins and DNA replication

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PCNA binding through a conserved motif

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Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA.

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A role for FEN-1 in nonhomologous DNA end joining: the order of strand annealing and nucleolytic processing events

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Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300

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