Insights Into The Recq Helicase Mechanism Revealed By The Structure Of The Helicase Domain Of Human Recql5

dc.creatorNewman
dc.creatorJoseph A.; Aitkenhead
dc.creatorHazel; Savitsky
dc.creatorPavel; Gileadi
dc.creatorOpher
dc.date2017
dc.dateabr
dc.date2017-11-13T13:56:31Z
dc.date2017-11-13T13:56:31Z
dc.date.accessioned2018-03-29T06:09:51Z
dc.date.available2018-03-29T06:09:51Z
dc.identifierNucleic Acids Research. Oxford Univ Press, v. 45, p. 4231 - 4243, 2017.
dc.identifier0305-1048
dc.identifier1362-4962
dc.identifierWOS:000399448400058
dc.identifier10.1093/nar/gkw1362
dc.identifierhttps://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw1362
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/329876
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1366901
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionRecQ helicases are important maintainers of genome integrity with distinct roles in almost every cellular process requiring access to DNA. RECQL5 is one of five human RecQ proteins and is particularly versatile in this regard, forming protein complexes with a diverse set of cellular partners in order to coordinate its helicase activity to various processes including replication, recombination and DNA repair. In this study, we have determined crystal structures of the core helicase domain of RECQL5 both with and without the nucleotide ADP in two distinctly different ('Open' and 'Closed') conformations. Small angle X-ray scattering studies show that the 'Open' form of the protein predominates in solution and we discuss implications of this with regards to the RECQL5 mechanism and conformational changes. We have measured the ATPase, helicase and DNA binding properties of various RECQL5 constructs and variants and discuss the role of these regions and residues in the various RECQL5 activities. Finally, we have performed a systematic comparison of the RECQL5 structures with other RecQ family structures and based on these comparisons we have constructed a model for the mechano-chemical cycle of the common catalytic core of these helicases.
dc.description45
dc.description7
dc.description4231
dc.description4243
dc.descriptionAbbVie
dc.descriptionBayer Pharma AG
dc.descriptionBoehringer Ingelheim
dc.descriptionCanada Foundation for Innovation
dc.descriptionEshelman Institute for Innovation
dc.descriptionGenome Canada
dc.descriptionInnovative Medicines Initiative (EU/EFPIA) [ULTRA-DD 115766]
dc.descriptionJanssen
dc.descriptionMerck Co.
dc.descriptionNovartis Pharma AG
dc.descriptionOntario Ministry of Economic Development and Innovation
dc.descriptionPfizer
dc.descriptionSao Paulo Research Foundation-FAPESP
dc.descriptionTakeda
dc.descriptionWellcome Trust [106169/ZZ14/Z]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageEnglish
dc.publisherOxford Univ Press
dc.publisherOxford
dc.relationNucleic Acids Research
dc.rightsaberto
dc.sourceWOS
dc.subjectBlooms Syndrome Helicase;rna-polymerase-ii;human Recq5-beta;replication Stress
dc.subjectHigh-resolution;breast-cancer;dna Helicase;cell-cycle;transcription;suppresses
dc.titleInsights Into The Recq Helicase Mechanism Revealed By The Structure Of The Helicase Domain Of Human Recql5
dc.typeArtículos de revistas


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