Determination of the relative and absolute stereochemistry of a potent and α1A-selective adrenoceptor antagonist

The binding affinities and selectivities of antagonists Figure 1 and Scheme 2 for the α_1A-adrenoceptor are dependent on the stereochemical orientation of the groups at the C-4 and C-5 positions of the oxazolidinone ring. The unambiguous assignment of the relative and absolute configurations of the diastereomers of SNAP 7915 (Figure 1 and Scheme 2) is reported.     

Membrane targeting of RecA during genetic transformation

Recombination in prokaryotes and eukaryotes is mediated by the RecA family of proteins. Although the interactions between RecA and DNA are well studied, the cellular location of these interactions is not known. Using genetic transformation of Streptococcus pneumoniae as a model system, there was increased expression of a protein, colligrin, and RecA, products of the rec locus during genetic transfer. These proteins formed a complex and were found associated with the membranes of genetically competent cells. With immunoelectron microscopy and subcellular fractionation, we showed that the induction of competence led to the translocation of RecA and colligrin to the membrane and to the formation of clusters of RecA in a colligrin-dependent step. Based on the behaviour of colligrin and RecA during genetic exchange and the numerous proteins in prokaryotes and eukaryotes with domains similar to colligrin, we suggest that there may exist a family of proteins, which gathers macromolecules at specific sites in biological membranes.     

Identification of a complex of the three forms of the rat liver asialoglycoprotein receptor

We have generated antibodies against synthetic peptides which represent the carboxyl terminus of either the major, or the two minor, forms of the rat hepatic lectin which recognizes galactose-terminated glycoproteins (asialoglycoproteins). The antibodies were shown to be specific for the form of the lectin containing the immunizing peptide sequence by the following: reaction with purified lectin after sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunoprecipitation of sodium dodecyl sulfate-denatured lectin, immunoprecipitation of lectin synthesized in vitro. These antibodies, however, precipitated all three rat hepatic lectin forms from nonionic detergent extracts of hepatocytes labeled with 125I via the lactoperoxidase catalyzed technique. A similar result was obtained if antibody was bound to intact cells prior to solubilization with detergent and collection of the immune complexes. We conclude that at least the plasma membrane-associated fraction of the rat hepatic lectin forms exists as a heterotypic complex.     

Castilleja chambersii (Scrophulariaceae), a new rare species from the northern Coast Range of Oregon

Castilleja chambersii is described from several collections made in the Coast Range of southwestern Clatsop County, Oregon. The new species is a member of subgenusCastilleja and is most closely related toC. parviflora andC. rupicola. This rare species is known from only three small and geographically restricted populations. Two new meiotic chromosome counts ofn=12 are reported for the new species.     

UDP-glucose: Indoleacetic acid glucosyl transferase and indoleacetyl-glucose: Myo-inositol indoleacetyl transferase

We have demonstrated the in vitro enzymatic synthesis of an ester of indole-3-acetic acid (IAA) and glucose and of IAA and myo-inositol by the following reaction sequence: lt]o| li]1) IAA + UDPG ? IAA-glucose +UDP li]2) IAA-glucose +myo-inositol → IAA-itmyo-inositol +glucose The enzymes were partially purified from extracts of immature kernels of Zea mays sweet corn and the two activities separated on a Sephadex G-150 column. Products were characterized, primarily, by comparison of their 70 eV mass spectra with those of authentic synthetic standards. To our knowledge this is the first example of enzymatically catalyzed acylation by a 1-O-acylsugar.     

Heat stress in the presence of low RNA polymerase activity increases chromosome copy number of Escherichia coli

Summary A temperature shift-up accompanied by a reduction in RNA polymerase activity in Escherichia coli causes an increased rate of initiation leading to a 1.7- to 2.2-fold increase in chromosome copy number. A temperature shift-up without a reduction in polymerase activity induces only a transient non-scheduled initiation of chromosome replication caused by heat shock with no detectable effect on chromosome copy number.