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dc.contributor.advisorEttrich, Rüdiger Horst
dc.contributor.authorSinha, Dhiraj
dc.date.accessioned2021-12-08T12:55:08Z
dc.date.available2021-12-08T12:55:08Z
dc.date.issued2017
dc.date.submitted2016-12-15
dc.identifier.urihttps://dspace.jcu.cz/handle/20.500.14390/33859
dc.format154 p.
dc.format154 p.
dc.language.isoeng
dc.publisherJihočeská univerzitacze
dc.rightsBez omezení
dc.subjectType I RM systemeng
dc.subjectEcoR124Ieng
dc.subjectPentameric complexeng
dc.subjectMotor subuniteng
dc.subjectHelicaseseng
dc.subjectInteractionseng
dc.subjectDomain motionseng
dc.subjectMolecular dynamicseng
dc.subjectPrincipal component analysiseng
dc.subjectSignal transfereng
dc.subjectTranslocase activityeng
dc.subjectEndonuclease activityeng
dc.titleInterdoménové a intradoménové interakce u motorové podjednotky EcoR124I: Výpočetní studiecze
dc.title.alternativeInter and intra domain interaction in the motor subunit of EcoR124I: A computational studyeng
dc.typedisertační prácecze
dc.identifier.stag45938
dc.description.abstract-translatedEcoR124I is a Type I restrictionmodification (RM) enzyme and as such forms multifunctional pentameric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on the motor subunit HsdR. When non-methylated invading DNA is recognized by the complex, two HsdR endonuclease/motor subunits start to translocate dsDNA without strand separation activity up to thousands base pairs towards the stationary enzyme while consuming  1 molecule of ATP per base pair advanced. Whenever translocation is stalled the HsdR subunits cleave the dsDNA nonspecifically far from recognition site. The X-ray crystal structure of HsdR of EcoR124I bound to ATP gave a first insight of structural/functional correlation in the HsdR subunit. The four domains within the subunit were found to be in a square planer arrangement. Computational modeling including molecular dynamics in combination with crystallography, point mutations, in vivo and in vitro assays reveals how interactions between these four domains contribute to ATP-dependent DNA translocation, DNA cleavage or inter-domain communication between the translocase and endonuclease activities.eng
dc.date.accepted2017-02-06
dc.description.departmentPřírodovědecká fakultacze
dc.thesis.degree-disciplineBiofyzikacze
dc.thesis.degree-grantorJihočeská univerzita. Přírodovědecká fakultacze
dc.thesis.degree-namePh.D.
dc.thesis.degree-programBiofyzikacze
dc.description.gradeDokončená práce s úspěšnou obhajoboucze
dc.contributor.refereeSpiwok, Vojtěch
dc.contributor.refereeStockner, Thomas
dc.contributor.refereeVenkatachalam, K. V.


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