The Prevalence of Sexual Abuse in Institutions: Results From a Representative Population-Based Sample in Germany

The lifetime prevalence of sexual abuse in institutional settings in Germany was examined in a sample representative of the general adult population (N = 2,437). Participants completed a survey on whether they had ever experienced such abuse, its nature (contact, noncontact, forced sexual, intercourse), the type of institution (e.g. school, club), and the relationship of perpetrator to victim (peer, caregiver, staff member). Overall, 3.1% of adult respondents (women: 4.8%, men: 0.8%) reported having experienced some type of sexual abuse in institutions. Adult women reported higher rates of all types than did men, with rates of 3.9% versus 0.8% for contact sexual abuse, 1.2% versus 0.3% for noncontact sexual abuse, and 1.7% versus 0.2% for forced sexual intercourse. We conclude that a remarkable proportion of the general population experiences sexual abuse in institutions, underscoring the need for development of protective strategies. Especially, schools seem to represent good starting points for primary prevention strategies

Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin–proteasome pathway

Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins such as Rad23 and Dsk2 mediate the delivery of polyubiquitinated proteins to the proteasome in the ubiquitin–proteasome pathway. We show here that budding yeast peptidyl-tRNA hydrolase 2 (Pth2), which was previously recognized as a peptidyl-tRNA hydrolase, is a UBL domain-binding protein that participates in the ubiquitin–proteasome pathway. Pth2 bound to the UBL domain of both Rad23 and Dsk2. Pth2 also interacted with polyubiquitinated proteins through the UBA domains of Rad23 and Dsk2. Pth2 overexpression caused an accumulation of polyubiquitinated proteins and inhibited the growth of yeast. Ubiquitin-dependent degradation was accelerated in the pth2Δ mutant and was retarded by overexpression of Pth2. Pth2 inhibited the interaction of Rad23 and Dsk2 with the polyubiquitin receptors Rpn1 and Rpn10 on the proteasome. Furthermore, Pth2 function involving UBL-UBA proteins was independent of its peptidyl-tRNA hydrolase activity. These results suggest that Pth2 negatively regulates the UBL-UBA protein-mediated shuttling pathway in the ubiquitin–proteasome system

Differences in dinucleotide frequencies of thermophilic genes encoding water soluble and membrane proteins

The occurrence frequencies of the dinucleotides of genes of three thermophilic and three mesophilic species from both archaea and eubacteria were investigated in this study. The genes encoding water soluble proteins were rich in the dinucleotides of purine dimers, whereas the genes encoding membrane proteins were rich in pyrimidine dimers. The dinucleotides of purine dimers are the counterparts of pyrimidine dimers in a double-stranded DNA. The purine/pyrimidine dimers were favored in the thermophiles but not in the mesophiles, based on comparisons of observed and expected frequencies. This finding is in agreement with our previous study which showed that purine/pyrimidine dimers are positive factors that increase the thermal stability of DNA. The dinucleotides AA, AG, and GA are components of the codons of charged residues of Glu, Asp, Lys, and Arg, and the dinucleotides TT, CT, and TC are components of the codons of hydrophobic residues of Leu, Ile, and Phe. This is consistent with the suitabilities of the different amino acid residues for water soluble and membrane proteins. Our analysis provides a picture of how thermophilic species produce water soluble and membrane proteins with distinctive characters: the genes encoding water soluble proteins use DNA sequences rich in purine dimers, and the genes encoding membrane proteins use DNA sequences rich in pyrimidine dimers on the opposite strand