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dc.contributor.advisorTichý, Martin
dc.contributor.authorSkotnicová, Petra
dc.date.accessioned2023-03-07T11:03:19Z
dc.date.available2023-03-07T11:03:19Z
dc.date.issued2019
dc.date.submitted2019-09-26
dc.identifier.urihttps://dspace.jcu.cz/handle/20.500.14390/40821
dc.format109
dc.format109
dc.language.isoeng
dc.publisherJihočeská univerzitacze
dc.rightsBez omezení
dc.subjectSynechocystiscze
dc.subjecttetrapyrrolová dráhacze
dc.subjecthemcze
dc.subjectchlorofylcze
dc.subjectpurifikace proteinucze
dc.subjectsupresorový mutantcze
dc.subjectprotoporfyrinogen oxidázacze
dc.subjectBtpAcze
dc.subjectSll1106cze
dc.subjectCurTcze
dc.subjectSynechocystiseng
dc.subjecttetrapyrrole pathwayeng
dc.subjecthemeeng
dc.subjectchlorophylleng
dc.subjectprotein purificationeng
dc.subjectsuppressor mutanteng
dc.subjectprotoporphyrinogen oxidaseeng
dc.subjectBtpAeng
dc.subjectSll1106eng
dc.subjectCurTeng
dc.titleProteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesiscze
dc.title.alternativeProteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesiseng
dc.typedisertační prácecze
dc.identifier.stag26799
dc.description.abstract-translatedThe goal of the thesis was to enhance our understanding of the tetrapyrrole pathway in cyanobacteria by a study of selected proteins involved in the pathway. During the project I have revealed functional connection between protoporphyrinogen IX oxidase HemJ and preceding enzyme in the pathway by complementation of protoporphyrinogen IX oxidase deletion mutant by its analog HemG from Escherichia coli. Heme b was identified as a cofactor of HemJ. Another protein deeply influencing tetrapyrrole accumulation, BtpA was found to form a complex with GluTR, the enzyme at the beginning of the tetrapyrrole pathway. Lastly, CurT protein, the component of the structures anticipated to function in PSII assembly and/or repair localized at plasma/thylakoid membrane interface, was co isolated with the enzymes of the tetrapyrrole pathway suggesting that the specific CurT containing membranes could be a place of both photosystem II assembly/repair and chlorophyll delivery.eng
dc.date.accepted2019-12-16
dc.description.departmentPřírodovědecká fakultacze
dc.thesis.degree-disciplineMolekulární a buněčná biologie a genetikacze
dc.thesis.degree-grantorJihočeská univerzita. Přírodovědecká fakultacze
dc.thesis.degree-namePh.D.
dc.thesis.degree-programMolekulární a buněčná biologiecze
dc.description.gradeDokončená práce s úspěšnou obhajoboucze
dc.contributor.refereeEaton-Rye, Julian
dc.contributor.refereeFischer, Lukáš


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