Original title: Light-harvesting like domain of the cyanobacterial ferrochelatase
Authors: PAZDERNÍK, Marek
Document type: Doctoral theses
Year: 2019
Language: eng
Abstract: This thesis is focused on elucidating the function of the C-terminal transmembrane lightharvesting complex like (LHC) domain of the cyanobacterial ferrochelatase (FeCh). Using the model cyanobacterium Synechocystis PCC 6803, I show that the FeCh LHC domain can bind chlorophyll (Chl) and carotenoids; however, this pigment binding occurs only when the biosynthesis of heme and Chl in the cell is misbalanced. Further, I found that point mutation, which prevents the pigment binding to FeCh LHC domain results in a misregulated ratio between heme and Chl during stress conditions due to low heme accumulation. My data also show that the FeCh LHC domain interacts with CurT protein most likely to localize the FeCh into a specialized membrane domain, where the synthesis of photosystem II is proposed to occur. Based on my data I propose that the role of the FeCh LHC domain is to monitor the availability of Chl during photosystem biogenesis and to coordinate Chl availability with the synthesis of heme.
Keywords: chlorophyll; ferrochelatase; heme; light-harvesting complex; tetrapyrrole pathway
Citation: PAZDERNÍK, Marek. Light-harvesting like domain of the cyanobacterial ferrochelatase. 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/45445

Permalink: http://www.nusl.cz/ntk/nusl-513499


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Universities and colleges > Public universities > University of South Bohemia in České Budějovice
Academic theses (ETDs) > Doctoral theses