Dokument

Summary:
The regulation of protein amounts in the cell is of utmost importance, as imbalance can lead to cell death. Hence, the protein levels are meticulously balanced by a vast network of regulation. This network penetrates all levels of regulation, from transcription to translation and post-translational modification. Messenger RNA (mRNA) maturation is a regulatory process at the post-transcriptional level and enables the cell to adapt to environmental changes quickly and resourcefully. In Bacillus subtilis, a soil-dwelling model organism, a large margin of mRNA maturation is carried out by the endoribonuclease RNase Y. However, the precise regulation of the maturation is still not well understood and only some factors involved in the regulation of RNase Y are known, such as the RicAFT complex. This complex is associated with the RNase Y in vivo and controls the maturation and degradation of a plethora of different mRNAs. Additionally, the complex is vital for the switch between lifestyles, as a dysfunctional complex leads to various phenotypes: flat and unstructured biofilms, dysfunctional sporulation, and loss of genetic competence. Additionally, the RicAFT complex could be involved in a regulatory cascade of proteins that activates all these processes, essentially regulating the same processes possibly in two different pathways. The switching between these lifestyles is vital for bacteria to survive in an everchanging environment. Hence, the RicAFT complex is a prime target for research, as it is conserved in Bacilli and many aspects of its role and function are unknown. Therefore, a biochemical and structural analysis of the complex is essential for understanding its function, which this work strives to achieve. Henceforth, various biochemical methods are employed to unravel its structure and its interaction sites. The complex is comprised of three proteins: RicA, RicF and RicT. These are not encoded in one operon yet form a stable complex. Their mechanism of interaction is unknown, as is the structure of the whole complex. However, it is known that the complex coordinates two [4Fe-4S] cluster and binds FADH, their role is yet to be determined. In this work, a comprehensive overview and biochemical analysis of the complex and its interactions is given.

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