Proteins involved in the tetrapyrrole pathway in Synechocystis sp. PCC 6803 and their localization in the proximity of PSII biogenesis

Mgr. Petra SKOTNICOVÁ

Disertační práce

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

Synechocystis, tetrapyrrolová dráha, hem, chlorofyl, purifikace proteinu, supresorový mutant, protoporfyrinogen oxidáza, BtpA, Sll1106, CurT

Jazyk práce: angličtina

Datum vytvoření / odevzdání či podání práce: 26. 9. 2019

Obhajoba závěrečné práce

• Obhajoba proběhla 16. 12. 2019
• Vedoucí: RNDr. Martin Tichý, Ph.D.

JIHOČESKÁ UNIVERZITA V ČESKÝCH BUDĚJOVICÍCH

Přírodovědecká fakulta

Doktorský studijní program / obor:
Molekulární a buněčná biologie / Molekulární a buněčná biologie a genetika