The structure of the acidic exopolysaccharide of Pseudomonas marginalis strains PF-05-2 and PM-LB-1

The structure of an acidic exopolysaccharide of two strains of Pseudomonas marginalis, a bacterium which causes soft rots of various vegetables, has been determined to consist of a repeating unit of: ----4) beta-D-Manp-(1----3)alpha-D-Glcp-(1----4)alpha-L-Rhap-(1-. The glucose is pyruvated at O-4 and O-6 and the mannose is acetylated at either O-2 or O-3.     

Yields of alginates produced by fluorescent pseudomonads in batch culture

Summary Saprophytic and plant pathogenic fluorescent pseudomonads are possible sources of bacterial alginates to be used as substitutes for algal alginates for certain commercial applications. In this study, a total of 115 strains of fluorescentPseudomonas species (P. cichorii, P. fiuorescens, P. syringae andP. viridiflava) were tested for yields of alginates when grown in batch culture in a proprietary liquid medium (PLM). The PLM contained either fructose or glucose (both at 5%, w/v) as the primary carbon and energy source. For comparison, selected strains were also grown in a modified Vogel and Bonner medium (MVBM) containing gluconate (5%, w/v) and formulated to support maximal alginate production by the human pathogenP. aeruginosa. After five days of incubation at 24°C with shaking (250–300 r.p.m.), alginates were harvested from the culture fluids by precipitation with three volumes of isopropanol. Maximum yields of alginates, based on assays for uronic acid content of precipitable material, were 5 g L^–1 for PLM with fructose, 3 g L^–1 for PLM with glucose and 9 g L^–1 for MVBM.Reference to a brand or firm name does not constitute an endorsement by the US Department of Agriculture over others of a similar nature not mentioned.     

Comparison of the effects of class 1 and class 2 heparin-binding growth factors on protein synthesis and actin mRNA expression in BALB/c-3T3 cells

Biological effects of class 1 or class 2 heparin-binding growth factors (HBGFs) were compared in BALB/c-3T3 cells. Changes in protein synthesis, as monitored by two-dimensional gel electrophoresis, reveal that while both HBGFs induce the same changes in the synthesis of intracellular proteins, class 2 HBGF selectively increases the synthesis of a 43-kD extracellular protein. Heparin, which potentiates the mitogenic activity of class 1 but not class 2 HBGF, does not potentiate the changes in protein synthesis elicited by HBGF-1. Since each HBGF increases actin synthesis, regulation of actin mRNA expression was examined. Actin mRNA levels increase rapidly and transiently in response to either HBGF, and similar superinduction responses are observed in the presence of HBGF and cycloheximide. Although the maximum increase in actin mRNA stimulated by either HBGF is similar, the levels of mRNA induced by class 2 HBGF remain elevated up to 48 hours compared to the level induced by class 1 HBGF. These results imply that in the same cell type class 1 and class 2 HBGFs may modulate some biological effects differently.     

The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors

We describe the nucleotide sequences of several overlapping cDNA clones specific for human glutaminyl-tRNA synthetase. The identified open reading frame indicates that the enzyme is composed of 1440 amino acids. A stretch of about 360 amino acids of the human enzyme is highly conserved in bacterial and yeast glutaminyl-tRNA synthetases. However, the human enzyme is three times larger than the bacterial and twice as large as the yeast enzyme suggesting that a considerable part of human glutaminyl-tRNA synthetase has evolved to perform functions other than the charging of tRNA. The sequence outside of the conserved core region includes three 57-amino acid repeats followed by a consecutive stretch of 11 charged amino acids. A computer assisted search of two protein data banks reveals that the human glutaminyl-tRNA synthetase shares small blocks of amino acid similarities with several other synthetases of different amino acid specificities. Interestingly, the enzyme also possesses some regions of similarities with eukaryotic translation elongation factor EF-1 but not with any other sequence stored in the protein data banks. The coding regions of human and mouse glutaminyl-tRNA synthetase cDNAs are identical at 94% of the codons. However, the 3'-noncoding regions of mouse and human mRNAs are more divergent (approximately 68%) but both possess the potential to form stable secondary structures of similar general architecture.     

C-terminal angiogenin peptides inhibit the biological and enzymatic activities of angiogenin

Synthetic peptides corresponding to the C-terminal region of angiogenin (Ang) inhibit the enzymatic and biological activities of the molecule while peptides from the N-terminal region do not affect either activity. The peptide Ang(108-121) transiently abolishes the inhibition of cell-free protein synthesis caused by angiogenin coincidentally with its cleavage of reticulocyte RNA. Several C-terminal peptides also inhibit nuclease activity of angiogenin when tRNA is the substrate. Furthermore, peptide Ang(108-123) significantly decreases neovascularization elicited by angiogenin in the chick chorioallantoic membrane assay.