Show simple item record

dc.contributor.authorFinger, L David
dc.contributor.authorAtack, John M
dc.contributor.authorTsutakawa, Susan
dc.contributor.authorClassen, Scott
dc.contributor.authorTainer, John
dc.contributor.authorGrasby, Jane
dc.contributor.authorShen, Binghui
dc.date.accessioned2013-05-02
dc.date.accessioned2017-03-01T22:25:44Z
dc.date.available2017-03-01T22:25:44Z
dc.date.issued2012
dc.date.modified2013-12-03T00:20:51Z
dc.identifier.issn0306-0225
dc.identifier.doi10.1007/978-94-007-4572-8_16
dc.identifier.urihttp://hdl.handle.net/10072/53212
dc.description.abstractProcessing of Okazaki fragments to complete lagging strand DNA synthesis requires coordination among several proteins. RNA primers and DNA synthesised by DNA polymerase α are displaced by DNA polymerase δ to create bifurcated nucleic acid structures known as 5′-flaps. These 5′-flaps are removed by Flap Endonuclease 1 (FEN), a structure-specific nuclease whose divalent metal ion-dependent phosphodiesterase activity cleaves 5′-flaps with exquisite specificity. FENs are paradigms for the 5′ nuclease superfamily, whose members perform a wide variety of roles in nucleic acid metabolism using a similar nuclease core domain that displays common biochemical properties and structural features. A detailed review of FEN structure is undertaken to show how DNA substrate recognition occurs and how FEN achieves cleavage at a single phosphate diester. A proposed double nucleotide unpairing trap (DoNUT) is discussed with regards to FEN and has relevance to the wider 5′ nuclease superfamily. The homotrimeric proliferating cell nuclear antigen protein (PCNA) coordinates the actions of DNA polymerase, FEN and DNA ligase by facilitating the hand-off intermediates between each protein during Okazaki fragment maturation to maximise through-put and minimise consequences of intermediates being released into the wider cellular environment. FEN has numerous partner proteins that modulate and control its action during DNA replication and is also controlled by several post-translational modification events, all acting in concert to maintain precise and appropriate cleavage of Okazaki fragment intermediates during DNA replication.
dc.description.peerreviewedNo
dc.description.publicationstatusYes
dc.format.extent298149 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherSubcellular Biochemistry
dc.publisher.placeBook
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom301
dc.relation.ispartofpageto-326
dc.relation.ispartofjournalSubcellular Biochemistry
dc.relation.ispartofvolume62
dc.rights.retentionY
dc.subject.fieldofresearchEnzymes
dc.subject.fieldofresearchcode310106
dc.titleThe wonders of flap endonucleases: structure, function, mechanism and regulation
dc.typeJournal article
dc.type.descriptionC2 - Articles (Other)
dc.type.codec2x
gro.facultyFaculty of Science, Environment, Engineering and Technology
gro.rights.copyright© 2012 Springer. This is the author-manuscript version of this paper. It is reproduced here in accordance with the copyright policy of the publisher. Please refer to the publisher’s website for further information.
gro.date.issued2012
gro.hasfulltextFull Text
gro.griffith.authorAtack, John M.


Files in this item

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record