Human MUS81 complexes stimulate flap endonuclease 1 (Q24318451)

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Tamir Amangyeld

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Tuan A Nguyen

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Palinda R Munashingha

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Yeon-Soo Seo

The DNA replication fork in eukaryotic cells.

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language of work or name

English

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publication date

July 2012

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published in

FEBS Journal

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volume

279

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issue

13

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page(s)

2412-30

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cites work

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Eukaryotic lagging strand DNA replication employs a multi-pathway mechanism that protects genome integrity

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Flap endonuclease 1: a central component of DNA metabolism

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Enzymatic completion of mammalian lagging-strand DNA replication

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RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes

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Involvement of Vts1, a structure-specific RNA-binding protein, in Okazaki fragment processing in yeast

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The MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing

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Genetic and functional interactions between Mus81-Mms4 and Rad27.

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In vivo and in vitro studies of Mgs1 suggest a link between genome instability and Okazaki fragment processing

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Dna2 on the road to Okazaki fragment processing and genome stability in eukaryotes

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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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Flap endonuclease homologs in archaebacteria exist as independent proteins.

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Functional regulation of FEN1 nuclease and its link to cancer

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Human replication factor C stimulates flap endonuclease 1

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

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Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1

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Damage tolerance protein Mus81 associates with the FHA1 domain of checkpoint kinase Cds1

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The Mechanism of Mus81-Mms4 Cleavage Site Selection Distinguishes It from the Homologous Endonuclease Rad1-Rad10

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Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed replication forks

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Functional overlap between Sgs1-Top3 and the Mms4-Mus81 endonuclease

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Structural and functional relationships of the XPF/MUS81 family of proteins

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Identification and characterization of the human mus81-eme1 endonuclease

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Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM.

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The 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysis

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The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations.

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Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate

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Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation

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Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathways

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Involvement of mammalian Mus81 in genome integrity and tumor suppression

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Disruption of murine Mus81 increases genomic instability and DNA damage sensitivity but does not promote tumorigenesis

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BLM helicase facilitates Mus81 endonuclease activity in human cells

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Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in human S-phase cells

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Crystal structure of the Mus81-Eme1 complex

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The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair

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Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family

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Characterization of human exonuclease 1 in complex with mismatch repair proteins, subcellular localization and association with PCNA

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The interaction of DNA mismatch repair proteins with human exonuclease I

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The characterization of a mammalian DNA structure-specific endonuclease

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inferred from DOI database lookup

7 January 2021

based on heuristic

Functional domains required for the Saccharomyces cerevisiae Mus81-Mms4 endonuclease complex formation and nuclear localization

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08620.X

inferred from DOI database lookup

7 January 2021

based on heuristic

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

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08620.X