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Writing travel, writing life
(2022)
The book compares the texts of three Swiss authors: Ella Maillart, Annemarie Schwarzenbach and Nicolas Bouvier. The focus is on their trip from Genève to Kabul that Ella Maillart and Annemarie Schwarzenbach made together in 1939/1940 and Nicolas Bouvier 1953/1954 with the artist Thierry Vernet. The comparison shows the strong connection between the journey and life and between ars vivendi and travel literature.
This book also gives an overview of and organises the numerous terms, genres, and categories that already exist to describe various travel texts and proposes the new term travelling narration. The travelling narration looks at the text from a narratological perspective that distinguishes the author, narrator, and protagonist within the narration.
In the examination, ten motifs could be found to characterise the travelling narration: Culture, Crossing Borders, Freedom, Time and Space, the Aesthetics of Landscapes, Writing and Reading, the Self and/as the Other, Home, Religion and Spirituality as well as the Journey. The importance of each individual motif does not only apply in the 1930s or 1950s but also transmits important findings for living together today and in the future.
Saccharomyces cerevisiae possesses two glycogenin isoforms (designated as Glg1p and Glg2p) that both contain a conserved tyrosine residue, Tyr232. However, Glg2p possesses an additional tyrosine residue, Tyr230 and therefore two potential autoglucosylation sites. Glucosylation of Glg2p was studied using both matrix-assisted laser desorption ionization and electrospray quadrupole time of flight mass spectrometry. Glg2p, carrying a C-terminal (His(6)) tag, was produced in Escherichia coli and purified. By tryptic digestion and reversed phase chromatography a peptide (residues 219-246 of the complete Glg2p sequence) was isolated that contained 4-25 glucosyl residues. Following incubation of Glg2p with UDPglucose, more than 36 glucosyl residues were covalently bound to this peptide. Using a combination of cyanogen bromide cleavage of the protein backbone, enzymatic hydrolysis of glycosidic bonds and reversed phase chromatography, mono- and diglucosylated peptides having the sequence PNYGYQSSPAM were generated. MS/MS spectra revealed that glucosyl residues were attached to both Tyr232 and Tyr230 within the same peptide. The formation of the highly glucosylated eukaryotic Glg2p did not favour the bacterial glycogen accumulation. Under various experimental conditions Glg2p-producing cells accumulated approximately 30% less glycogen than a control transformed with a Glg2p lacking plasmid. The size distribution of the glycogen and extractable activities of several glycogen-related enzymes were essentially unchanged. As revealed by high performance anion exchange chromatography, the intracellular maltooligosaccharide pattern of the bacterial cells expressing the functional eukaryotic transgene was significantly altered. Thus, the eukaryotic glycogenin appears to be incompatible with the bacterial initiation of glycogen biosynthesis