About: Importance of homo-dimerization of Fanconi-associated nuclease 1 in DNA flap cleavage

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About: Importance of homo-dimerization of Fanconi-associated nuclease 1 in DNA flap cleavage Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Importance of homo-dimerization of Fanconi-associated nuclease 1 in DNA flap cleavage
Creator	Xiong, Yong Aihara, Hideki Longerich, Simonne Rao, Timsi Sung, Patrick Zhao, Weixing
Source	BioRxiv
abstract	Fanconi-associated nuclease 1 (FAN1) removes interstrand DNA crosslinks (ICLs) through its DNA flap endonuclease and exonuclease activities. Crystal structures of human and bacterial FAN1 bound to a DNA flap have been solved. The Pseudomonas aeruginosa bacterial FAN1 and human FAN1 (hFAN1) missing a flexible loop are monomeric, while intact hFAN1 is homo-dimeric in structure. Importantly, the monomeric and dimeric forms of FAN1 exhibit very different DNA binding modes. Here, we interrogate the functional differences between monomeric and dimeric forms of FAN1 and provide an explanation for the discrepancy in oligomeric state between the two hFAN1 structures. Specifically, we show that the flexible loop in question is needed for hFAN1 dimerization. While monomeric and dimeric bacterial or human FAN1 proteins cleave a short 5’ flap strand with similar efficiency, optimal cleavage of a long 5’ flap strand is contingent upon protein dimerization. Our study therefore furnishes biochemical evidence for a role of hFAN1 homodimerization in biological processes that involve 5’ DNA Flap cleavage.
has issue date	2017-12-18(xsd:dateTime)
bibo:doi	10.1101/236208
has license	biorxiv
sha1sum (hex)	2143e20841789cf867167954dff54ca7e684add8
schema:url	https://doi.org/10.1101/236208
resource representing a document's title	Importance of homo-dimerization of Fanconi-associated nuclease 1 in DNA flap cleavage
schema:publication	bioRxiv
resource representing a document's body	covid:2143e20841789cf867167954dff54ca7e684add8#body_text
is schema:about of	named entity 'long' named entity 'domain' named entity 'crosslinks' named entity 'flexible' named entity 'loop' named entity 'needed' named entity 'homodimerization' named entity 'dimerization' named entity 'DNA' named entity 'SAP' named entity 'PANEL' named entity 'ASPARTATE' named entity 'STATE' named entity 'RED' named entity 'efficiency' named entity 'light scattering' named entity 'human' named entity 'DNA' named entity 'PDB' named entity 'functional' named entity 'proteins' named entity 'Flap' named entity 'monomeric' named entity 'structure' named entity 'cleavage' named entity 'strand' named entity 'flap' named entity 'biochemical' named entity 'cleavage' named entity 'chromatographic' named entity 'FAN1' named entity 'cleavage' named entity 'light scattering' named entity 'FAN1' named entity 'DNA binding' named entity 'PDB' named entity 'monomer' named entity 'molecule' named entity 'cleavage' named entity 'FAN1' named entity 'dimerization' named entity 'dimerization' named entity 'substrates' named entity 'nuclease' named entity 'substrate' named entity 'protomers' named entity 'replication forks' named entity 'nuclease' named entity 'physiological' named entity 'DNA-binding' named entity 'crystal structures' named entity 'SEC' named entity 'cleavage pattern' named entity 'dimer' named entity 'ICLs' named entity 'FAN1' named entity 'enzyme' named entity 'dimeric structure' named entity 'ssDNA' named entity 'size exclusion chromatography' named entity 'substrates' named entity 'exonuclease' named entity 'dimer' named entity 'multi-angle laser light scattering' named entity 'Vibrio' named entity 'ssDNA' named entity 'MALLS' named entity 'Fanconi' named entity 'substrate' named entity 'protomers' named entity 'SEC' named entity 'orthologs' named entity 'Pseudomonas aeruginosa' named entity 'FAN1' named entity 'FAN1' named entity 'FAN1' named entity 'DNA binding' named entity 'protein' named entity 'single-stranded'

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