Transforming a set of biological flat file librariesto a fast access network

SRS (Sequence Retrieval System), an indexing system for flatfile libraries, provides fast access to individual library entriesvia retrie by keywords from rious data fields. SRS is now alsoable to build indices using cross–references that mostlibraries provide. Fifteen libraries of DNA and protein sequencesand structures have been selected. These libraries interactwith at least one other by means of cross–references.Indexing these cross–references allows a complete networkof libraries to be built. In the network an entry from one librarycan be linked in principle to every other library. If two librariesare not directly cross–referenced, the linkage can bemade with a succession of single links between neighbouring,cross–referenced libraries. A new operator has been addedto the query language of SRS for convenient specification oflinks amongst complete libraries or entry sets generated byprevious queries on particular libraries. All the informationin the network can now be used to retrieve an entry in a specificlibrary, e.g. the full information given in amino acid sequenceentries from SwissProt can now be used to retrieve related tertiarystructure entries from PDB. Furthermore, a search in a singlelibrary can be extended to a search in the complete librarynetwork, e.g. all entries in all databases pertaining to elastasecan be found.     

Point mutations in the 23 S rRNA genes of four lincomycin resistant Nicotiana plumbaginifolia mutants could provide new selectable markers for chloroplast transformation

Summary Experiments designed to establish stable chloroplast transformation require selectable marker genes encoded by the chloroplast genome. The antibiotic lincomycin is a specific inhibitor of chloroplast ribosomal activity and is known to bind to the large ribosomal subunit. We have investigated a defined region of the chloroplast 23 S rRNA genes from four lincomycin resistant Nicotiana plumbaginifolia mutants and from wild-type N. plumbaginifolia. The mutants LR415, LR421 and LR446 have A to G transitions at positions equivalent to the nucleotides 2058 and 2059 in the Escherichia coli 23 S rRNA. The mutant, LR400, possesses a G to A transition at a position corresponding to nucleotide 2032 of the E. coli 23 S rRNA.     

Design and operation of pulsed anaerobic digesters

The development of a pulse-driven loop reactor (PDLR), a pulsed anaerobic filter (PAF) and a pulsed anaerobic baffled reactor (PABR) is described. In an anaerobic PDLR internal circulation is achieved by a specially designed pulse-nozzle. In a PAF and PABR an oscillation is superimposed onto the liquid content of the fermenters by means of a pulse pump without any moving devices in the reactors. Pulsed digesters faciliate degassing, avoid reactor clogging as well as short-circuiting and allow a variety of packed-bed to fluidized-bed operations. Anaerobic fermentation of acetic acid and distillery slops in pulsed digesters on a laboratory scale shows that hydrodynamic stress caused by pulsation is well compatible to degrading bacteria.List of Symbols PAF Pulsed Anaerobic Filter - PDLR Pulse-Driven Loop Reactor - PABR Pulsed Anaerobic Baffled Reactor     

VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells.

In simple epithelial cells, apical and basolateral proteins and lipids in transit to the cell surface are sorted in the trans-Golgi network. We have recently isolated detergent-insoluble complexes from Madin-Darby canine kidney cells that are enriched in glycosphingolipids, apical cargo and a subset of the proteins of the exocytic carrier vesicles. The vesicular proteins are thought to be involved in protein sorting and include VIP21-caveolin. The vesicular protein VIP36 (36 kDa vesicular integral membrane protein) has been purified from a CHAPS-insoluble residue and a cDNA encoding VIP36 has been isolated. The N-terminal 31 kDa luminal/exoplasmic domain of the encoded protein shows homology to leguminous plant lectins. The transiently expressed protein is localized to the Golgi apparatus, endosomal and vesicular structures and the plasma membrane, as predicted for a protein involved in transport between the Golgi and the cell surface. It is diffusely localized on the plasma membrane but can be redistributed by antibody modulation into caveolae and clathrin-coated pits. We speculate that VIP36 binds to sugar residues of glycosphingolipids and/or glycosylphosphatidyl-inositol anchors and might provide a link between the extracellular/luminal face of glycolipid rafts and the cytoplasmic protein segregation machinery.     

Partial trisomy 2p due to a familial translocation 2/6. Cytogenetic and clinical case with special reference to ophthalmologic changes]

A translocation 2/6 inherited for 3 generations is described. The propositus, carrier of a partial trisomy 2p, showed multiple morphological anomalies of which microphtalmus and persistance of primary vitreous body were of particular interest. Based on a comparison of this with seven other patients in the literature, the most characteristic clinical symptoms of partial trisomy 2p are concluded to be the following: abundant lanugo at birth, glabella prominence, anteverted nares, dermatoglyphic anomalies, and malformations of the eyes.     

Structural basis for adaptation of lactobacilli to gastrointestinal mucus

The mucus layer covering the gastrointestinal (GI) epithelium is critical in selecting and maintaining homeostatic interactions with our gut bacteria. However, the underpinning mechanisms of these interactions are not understood. Here, we provide structural and functional insights into the canonical mucus‐binding protein (MUB), a multi‐repeat cell‐surface adhesin found in Lactobacillus inhabitants of the GI tract. X‐ray crystallography together with small‐angle X‐ray scattering demonstrated a ‘beads on a string’ arrangement of repeats, generating 174 nm long protein fibrils, as shown by atomic force microscopy. Each repeat consists of tandemly arranged Ig‐ and mucin‐binding protein (MucBP) modules. The binding of full‐length MUB was confined to mucus via multiple interactions involving terminal sialylated mucin glycans. While individual MUB domains showed structural similarity to fimbrial proteins from Gram‐positive pathogens, the particular organization of MUB provides a structural explanation for the mechanisms in which lactobacilli have adapted to their host niche by maximizing interactions with the mucus receptors, potentiating the retention of bacteria within the mucus layer. Together, this study reveals functional and structural features which may affect tropism of microbes across mucus and along the GI tract, providing unique insights into the mechanisms adopted by commensals and probiotics to adapt to the mucosal environment.