Family oblige: the link between CSR and succession intention in small and medium family firms.

This study investigates how family continuation, namely family tradition and succession intention, alter the socially responsible behavior of small and medium sized (SME) family firms. Using a unique dataset, we have conducted multiple regressions on survey data from German family SMEs and show a statistically and economically significant increase in Corporate Social Responsibility (CSR) alongside the planning of family succession. However, when analyzing the different facets of CSR, we have found strong variances: While succession intention goes along with an increased community, market, and supply chain engagement this is not the case for CSR directed towards employees, or the environment. Family tradition didn't correlate with a change in CSR behaviour to a relevant extent. In our theoretical embedding we employed socio-emotional wealth (SEW) theory to explain our findings. Thereby, our study fills a gap in the literature adding the perspective of SME family firms on the use of CSR in the context of family succession and also adding to the theoretical understanding of SEW.

Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp.

The "seventeen kilodalton protein" (Skp) is a predominant periplasmic chaperone of Escherichia coli, which is involved in the biogenesis of abundant outer membrane proteins (OMPs) such as OmpA, PhoE, and LamB. In this study the substrate profile of Skp was investigated in a proteomics approach. Skp was overexpressed in a deficient E. coli strain as a fusion protein with the Strep-tag and captured, together with any host proteins associated with it, from the periplasmic cell extract under mild conditions via one-step Strep-Tactin affinity chromatography. Copurified substrate proteins were then identified by high resolution 2-DE with immobilized pH-gradients, followed by MALDI-TOF MS. Apart from the known Skp substrates, including OmpA and LamB, more than 30 other interacting proteins were detected, especially from the outer membrane, among these FadL and BtuB, and from the periplasm such as MalE and OppA. Thus, Skp does not only serve as a specialized chaperone for a small set of OMPs, but it seems to exhibit a broader substrate spectrum, including soluble periplasmic proteins. These findings should prompt further investigation into the physiological role of Skp and may promote its use for the bacterial production of biochemically active heterologous proteins whose folding requires secretion into the oxidizing milieu of the periplasm.