Helicobacter pylori was identified in human liver tissue by PCR, hybridization, and partial DNA sequencing. Liver biopsies were obtained from patients with primary sclerosing cholangitis (n = 12), primary biliary cirrhosis (n = 12), and noncholestatic liver cirrhosis (n = 13) and (as controls) normal livers (n = 10). PCR analyses were carried out using primers for the Helicobacter genus, Helicobacter pylori(the gene encoding a species-specific 26-kDa protein and the 16S rRNA),Helicobacter bilis, Helicobacter pullorum, andHelicobacter hepaticus. Samples from patients with primary biliary cirrhosis and primary sclerosing cholangitis (11 and 9 samples, respectively) were positive by PCR with Helicobactergenus-specific primers. Of these 20 samples, 8 were positive with the 16S rRNA primer and 9 were positive with the 26-kDa protein primer ofH. pylori. These nine latter samples were also positive by Southern blot hybridization for the amplified 26-kDa fragment, and four of those were verified to be H. pylori by partial 16S rDNA sequencing. None of the samples reacted with primers for H. bilis, H. pullorum, or H. hepaticus. None of the normal livers had positive results in theHelicobacter genus PCR assay, and only one patient in the noncholestatic liver cirrhosis group, a young boy who at reexamination showed histological features suggesting primary sclerosing cholangitis, had a positive result in the same assay. Helicobacterpositivity was thus significantly more common in patients with cholestatic diseases (20 of 24) than in patients with noncholestatic diseases and normal controls (1 of 23) (P = <0.00001). Patients positive for Helicobacter genus had significantly higher values of alkaline phosphatases and prothrombin complex than Helicobacter-negative patients (P = 0.0001 and P = 0.0003, respectively). Among primary sclerosing cholangitis patients,Helicobacter genus PCR positivity was weakly associated with ulcerative colitis (P = 0.05). Significant differences related to blood group or HLA status were not found.

The Bacillus subtilis glpD gene encodes glycerol-3-phosphate dehydrogenase. This gene is preceded by a leader region containing an inverted repeat which acts as a transcription terminator. Expression of glpD is controlled by antitermination of transcription at the inverted repeat. Antitermination is effected by the glpP gene product in conjunction with glycerol-3-phosphate and, consequently, GlpP mutants fail to grow on glycerol as a sole carbon and energy source. We have isolated a number of glycerol-positive revertants of GlpP mutants. Most of these revertants have mutations in the inverted repeat of the glpD leader and produce glycerol-3-phosphate dehydrogenase constitutively. Unlike wild-type bacteria, they are not sensitive to glucose repression of glpD. A few of the revertants are temperature sensitive, i.e. they grow on glycerol at 32 degrees C but not at 45 degrees C and produce glycerol-3-phosphate dehydrogenase only at 32 degrees C. Northern blot analyses demonstrated that the temperature-sensitive expression of glpD is due to destabilization of glpD mRNA. Furthermore, introduction of the wild-type glpP gene into the revertants stabilized the glpD mRNA. This is probably a result of a direct interaction between the GlpP protein and the leader of glpD mRNA. Besides its function in antitermination of transcription of glpD, it is suggested that GlpP is also involved in controlling glpD mRNA stability. Introduction of the glpP gene into the revertants also restored glucose repression, indicating that this repression is mediated by the GlpP protein.

The Bacillus subtilis glpD gene encodes glycerol-3-phosphate (G3P) dehydrogenase. Expression of glpD is mainly controlled by termination/antitermination of transcription at an inverted repeat in the glpD leader. Antitermination is mediated by the antiterminator protein GlpP in the presence of G3P. In this paper, interaction between GlpP and glpD leader mRNA in vivo and in vitro is reported. In vivo, the antiterminating effect of GlpP can be titrated in a strain carrying the glpD leader on a plasmid. GlpP has been purified and gel shift experiments have shown that it binds to glpD leader mRNA in vitro. GlpP is not similar to other known antiterminator proteins, but database searches have revealed an Escherichia coli ORF which has a high degree of similarity to GlpP.

Expression of the Bacillus subtilis glpD gene, which encodes glycerol-3-phosphate (G3P) dehydrogenase, is controlled by termination or antitermination of transcription. The untranslated leader sequence of glpD contains an inverted repeat that gives rise to a transcription terminator. In the presence of G3P, the antiterminator protein GlpP binds to glpD leader mRNA and promotes readthrough of the terminator. Certain mutations in the inverted repeat of the glpD leader result in GlpP-independent, temperature-sensitive (TS) expression of glpD. The TS phenotype is due to temperature-dependent degradation of the glpD mRNA. In the presence of GlpP, the glpD mRNA is stabilized. glpD leader-lacZ fusions were integrated into the chromosomes of B. subtilis and Escherichia coli. Determination of steady-state levels of fusion mRNA in B. subtilis showed that the stability of the fusion mRNA is determined by the glpD leader part. Comparison of steady-state levels and half-lives of glpD leader-lacZ fusion mRNA in B. subtilis and E. coli revealed significant differences. A glpD leader-lacZ fusion transcript that was unstable in B. subtilis was considerably more stable in E. coli. GlpP, which stabilizes the transcript in B. subtilis, did not affect its stability in E. coli. Primer extension analysis showed that the glpD leader-lacZ fusion transcript is processed differently in B. subtilis and in E. coli. The dominating cleavage site in E. coli was barely detectable in B. subtilis. This site was shown to be a target of E. coli RNase III.The steady-state level of mRNA in a cell is a function of the rate of mRNA synthesis and the rate of its decay. For bacteria, there is a wealth of information on the regulation of mRNA synthesis (see, e.g., reference 27), while much less is known about mechanisms of mRNA decay (5,6,35).Most of our knowledge about bacterial mRNA decay is based on studies of Escherichia coli (26,34). In a simple model, an initial endoribonucleolytic attack at the 5Ј end of an mRNA opens up the molecule for internal downstream cleavages and the fragments generated are subsequently degraded by exoribonucleases (12). The initial cleavage is performed by one of two endoribonucleases, RNase E, encoded by the rne gene (7), or RNase III, encoded by the rnc gene (3,8). The endonucleolytic activity of RNase E is localized to the N-terminal half of the protein, which, unlike the C-terminal half, is essential for E. coli viability (29, 31). RNase III is primarily involved in maturation of stable RNA but also in degradation of some mRNA species. The hydrolytic exoribonuclease RNase II and the phosphorolytic exoribonuclease polynucleotide phosphorylase (PNPase) are important for the final (3Ј-to-5Ј) degradation of an mRNA to mono-and oligonucleotides. For a few E. coli mRNA species, binding of specific proteins has been found to have a decisive influence on mRNA half-life (28, 43).Much less is known about mRNA degradation in Bacillus subtilis. In several bacterial species, but not B. subtilis, sequence homologues to the N-termina...

Our paper is based on the Swiss research project ‘Interpreting in Medical Settings: Roles, Requirements and Responsibility’, which was supported by a grant of the Swiss Commission for Technology and Innovation (KTI) and carried out by an interdisciplinary team comprising medical specialists from the University Hospital of Basel (Marina Sleptsova and colleagues) and interpreting studies/applied linguistics researchers from the Zurich University of Applied Sciences (ZHAW) (Gertrud Hofer and colleagues). It explores videotape transcriptions of 12 authentic interpreted conversations between German speaking doctors/medical staff and patients of Turkish or Albanian origin. The analysis finds that culture-specific expressions produced by the patients occur rarely and do not pose any interpreting problems. By contrast, phatic tokens and hedges play an important role in medical personnel’s presentation of their interactional, trust building, diagnostic and therapeutic intentions. Although these expressions are essential communication elements geared at building patients’ compliance and establishing doctors’ safeguards, they are rarely or inconsistently rendered by the interpreters. It is argued that, while medical interpreters may have plausible reasons not to render these expressions, they would still need to be made aware of the significance of such pragmatic aspects of communication in training courses and/or pre-encounter briefings. More generally, empirical research – similar to that on questioning style and questioning techniques – should focus more on the exploration of discourse markers, meta-discourse comments and rapport-building expressions of different types of utterance and discourse practices in healthcare interpreting settings.