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Original title:
Proteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesis
Authors: SKOTNICOVÁ, Petra
Document type: Doctoral theses
Year: 2019
Language: eng
Abstract: The 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.
Keywords: BtpA; chlorofyl; CurT; hem; protoporfyrinogen oxidáza; purifikace proteinu; Sll1106; supresorový mutant; Synechocystis; tetrapyrrolová dráha
Citation: SKOTNICOVÁ, Petra. Proteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesis. České Budějovice, 2019. disertační práce (Ph.D.). JIHOČESKÁ UNIVERZITA V ČESKÝCH BUDĚJOVICÍCH. Přírodovědecká fakulta
Institution: University of South Bohemia in České Budějovice (web)
Document availability information: Fulltext is available in the Digital Repository of University of South Bohemia.
Original record: http://www.jcu.cz/vskp/26799
Permalink: http://www.nusl.cz/ntk/nusl-513393
The record appears in these collections:
Universities and colleges > Public universities > University of South Bohemia in České Budějovice
Academic theses (ETDs) > Doctoral theses
Authors: SKOTNICOVÁ, Petra
Document type: Doctoral theses
Year: 2019
Language: eng
Abstract: The 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.
Keywords: BtpA; chlorofyl; CurT; hem; protoporfyrinogen oxidáza; purifikace proteinu; Sll1106; supresorový mutant; Synechocystis; tetrapyrrolová dráha
Citation: SKOTNICOVÁ, Petra. Proteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesis. České Budějovice, 2019. disertační práce (Ph.D.). JIHOČESKÁ UNIVERZITA V ČESKÝCH BUDĚJOVICÍCH. Přírodovědecká fakulta
Institution: University of South Bohemia in České Budějovice (web)
Document availability information: Fulltext is available in the Digital Repository of University of South Bohemia.
Original record: http://www.jcu.cz/vskp/26799
Permalink: http://www.nusl.cz/ntk/nusl-513393
The record appears in these collections:
Universities and colleges > Public universities > University of South Bohemia in České Budějovice
Academic theses (ETDs) > Doctoral theses
Record created 2023-01-15, last modified 2023-03-12