Vom Mitgefühl zur Fairness: Michael Tomasello schreibt eine Naturgeschichte der menschlichen Moral

Michael Tomasello: Eine Naturgeschichte der menschlichen Moral. Frankfurt am Main: Suhrkamp Verlag 2016. 978-3-518-58695-

Erst kommt das Fressen: Kerstin Jacobsson und Jonas Lindblom betrachten den Tierschutzaktivismus aus moralsoziologischer Perspektive

Kerstin Jacobsson / Jonas Lindblom: Animal Rights Activism: A Moral-Sociological Perspective on Social Movements. Amsterdam: Amsterdam University Press 2017. 978-908964764

Hoffnungsvoll in eine ungewisse Zukunft: Rezension zu "Radikale Hoffnung: Ethik im Angesicht kultureller Zerstörung" von Jonathan Lear

Jonathan Lear: Radikale Hoffnung: Ethik im Angesicht kultureller Zerstörung. Berlin: Suhrkamp 2021. 978-3-518-58759-

Das höchste Gut: Didier Fassin versucht sich an einer Analyse der Ungleichheit menschlicher Leben

Didier Fassin: Das Leben: Eine kritische Gebrauchsanweisung. Berlin: Suhrkamp 2017. 978-3-518-58710-

Die Macht der Stimmungen: Heinz Bude über Stimmungen in Deutschland und Stimmung als soziologische Schlüsselkategorie

Heinz Bude: Das Gefühl der Welt: Über die Macht von Stimmungen. München: Hanser 2016. 978344625065

Internationalisierung der Curricula an Hochschulen für angewandte Wissenschaften: am Beispiel der Hochschule für Technik und Wirtschaft Dresden - University of Applied Sciences

Im folgenden Beitrag werden Möglichkeiten der internationalen Gestaltung der Curricula an der Hochschule für Technik und Wirtschaft Dresden – University of Applied Sciences (HTW Dresden) unter dem Ansatz „regional verankert und international orientiert“ dargestellt. Ziel des Prozesses ist die Suche nach einem Weg zur Internationalisierung, der die Profilierung der Hochschule stärkt und nicht verändert

An archaeal family-B DNA polymerase variant able to replicate past DNA damage: occurrence of replicative and translesion synthesis polymerases within the B family

A mutant of the high fidelity family-B DNA polymerase from the archaeon Thermococcus gorgonarius (Tgo-Pol), able to replicate past DNA lesions, is described. Gain of function requires replacement of the three amino acid loop region in the fingers domain of Tgo-Pol with a longer version, found naturally in eukaryotic Pol zeta (a family-B translesion synthesis polymerase). Inactivation of the 3'–5' proofreading exonuclease activity is also necessary. The resulting Tgo-Pol Z1 variant is proficient at initiating replication from base mismatches and can read through damaged bases, such as abasic sites and thymine photo-dimers. Tgo-Pol Z1 is also proficient at extending from primers that terminate opposite aberrant bases. The fidelity of Tgo-Pol Z1 is reduced, with amarked tendency tomake changes at G:C base pairs. Together, these results suggest that the loop region of the fingers domain may play a critical role in determining whether a family-B enzyme falls into the accurate genome-replicating category or is an errorprone translesion synthesis polymerase. Tgo-Pol Z1 may also be useful for amplification of damaged DNA

The novel Fh8 and H fusion partners for soluble protein expression in Escherichia coli : a comparison with the traditional gene fusion technology

The Escherichia coli host system is an advantageous choice for simple and inexpensive recombinant protein production but it still presents bottlenecks at expressing soluble proteins from other organisms. Several efforts have been taken to overcome E. coli limitations, including the use of fusion partners that improve protein expression and solubility. New fusion technologies are emerging to complement the traditional solutions. This work evaluates two novel fusion partners, the Fh8 tag (8 kDa) and the H tag (1 kDa), as solubility enhancing tags in E. coli and their comparison to commonly used fusion partners. A broad range comparison was conducted in a small-scale screening and subsequently scaled-up. Six difficult-to-express target proteins (RVS167, SPO14, YPK1, YPK2, Frutalin and CP12) were fused to eight fusion tags (His, Trx, GST, MBP, NusA, SUMO, H and Fh8). The resulting protein expression and solubility levels were evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis before and after protein purification and after tag removal. The Fh8 partner improved protein expression and solubility as the well-known Trx, NusA or MBP fusion partners. The H partner did not function as a solubility tag. Cleaved proteins from Fh8 fusions were soluble and obtained in similar or higher amounts than proteins from the cleavage of other partners as Trx, NusA or MBP. The Fh8 fusion tag therefore acts as an effective solubility enhancer, and its low molecular weight potentially gives it an advantage over larger solubility tags by offering a more reliable assessment of the target protein solubility when expressed as a fusion protein.The financial support of the EMBL Heidelberg, Germany and Fundacao para a Ciencia e Tecnologia (FCT), Portugal, is acknowledged: the fellowship SFRH/BD/46482/2008 to Sofia J. Costa and the project PTDC/CVT/103081/2008. The authors wish to acknowledge Anne-Claude Gavin for providing four of the constructs for this study (RVS167, SPO14, YPK1, and YPK2) and Emmanuel Poilpre for the experimental help (both from the EMBL Heidelberg, Germany)