Molecular aspects of gene transfer and foreign DNA acquisition in prokaryotes with regard to safety issues.

Horizontal gene transfer (HGT) is part of prokaryotic life style and a major factor in evolution. In principle, any combinations of genetic information can be explored via HGT for effects on prokaryotic fitness. HGT mechanisms including transformation, conjugation, transduction, and variations of these plus the role of mobile genetic elements are summarized with emphasis on their potential to translocate foreign DNA.

Profiling of alterations in platelet proteins during storage of platelet concentrates.

Background: The quality of platelet concentrates (PCs) is primarily determined in vitro by selective methods (e.g., pH, aggregometry), which provide only limited information on certain platelet (PLT) characteristics.

Proteomics as a tool for assessment of therapeutics in transfusion medicine: evaluation of prothrombin complex concentrates.

Background: Proteomic technologies are evolving tools to analyze complex protein patterns that to date have been rarely applied to transfusion medicine. The analysis of prothrombin complex concentrates (PCCs) was used as a model to evaluate to what extent these technologies can detect differences in blood-derived therapeutics beyond that of standard quality control.

Study Design And Methods: Three PCCs (two batches each) were individually analyzed for differences in protein content by functional assays, two-dimensional gel electrophoresis, and mass spectrometry.

RsbV-independent induction of the SigB-dependent general stress regulon of Bacillus subtilis during growth at high temperature.

General stress proteins protect Bacillus subtilis cells against a variety of environmental insults. This adaptive response is particularly important for nongrowing cells, to which it confers a multiple, nonspecific, and preemptive stress resistance. Induction of the general stress response relies on the alternative transcription factor, SigB, whose activity is controlled by a partner switching mechanism that also involves the anti-sigma factor, RsbW, and the antagonist protein, RsbV.

Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C.

RsbU is a positive regulator of the activity of sigmaB, the general stress-response sigma factor of Gram+ microorganisms. The N-terminal domain of this protein has no significant sequence homology with proteins of known function, whereas the C-terminal domain is similar to the catalytic domains of PP2C-type phosphatases. The phosphatase activity of RsbU is stimulated greatly during the response to stress by associating with a kinase, RsbT.

Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to low-temperature adaptation.

A variety of environmental and metabolic cues trigger the transient activation of the alternative transcription factor SigB of Bacillus subtilis, which subsequently leads to the induction of more than 150 general stress genes. This general stress regulon provides nongrowing and nonsporulated cells with a multiple, nonspecific, and preemptive stress resistance. By a proteome approach we have detected the expression of the SigB regulon during continuous growth at low temperature (15 degrees C).