Long-term bird colonization and turnover in restored woodlands

The long-term effectiveness of restored areas for biodiversity is poorly known for the majority of restored ecosystems worldwide. We quantified temporal changes in bird occurrence in restoration plantings of different ages and geometries, and compared observed patterns with a reference dataset from woodland remnants on the same farms as our plantings. Over time, bird species richness remained unchanged in spring but exhibited modest increases in winter. We found that wider plantings supported significantly greater bird species richness in spring and winter than narrow plantings. There was no evidence of a significant interaction between planting width and time. We recorded major temporal changes in the occurrence of a range of individual species that indicated a clear turnover of species as plantings matured. Our results further revealed marked differences in individual species occurrence between plantings and woodland remnants. Life-history attributes associated with temporal changes in the bird assemblage were most apparent in winter survey data, and included diet, foraging and nesting patterns, movement behaviour (e.g. migratory vs. dispersive), and body size. Differences in bird assemblages between plantings of different ages suggest that it is important that farms support a range of age classes of planted woodland, if the aim is to maximize the number of native bird species in restored areas. Our data also suggest that changes in the bird species occupying plantings of different ages can be anticipated in a broadly predictable way based on planting geometry (especially width) and key life-history attributes, particularly movement patterns and habitat and diet specialisation.     

Bacillus licheniformis 749-C plasma membrane penicillinase, a hydrophobic polar protein

Plasma membrane penicillinase from Bacillus licheniformis 749/C is hydrophobic in nature, although it is virtually identical to its riydrophilic exoenzyme counterpart in amino acid composition and sequence. Unlike the exoenzyme, however, the purified membrane enzyme retains [³³P]phosphate and [³H]glycerol. By isoelectricfocusing the membrane enzyme is more acidic than the exoenzyme; it has a lower mobility in SDS gel electrophoresis, consistent with the presence of a very hydrophobic moiety. Unlike the exoenzyme, which binds no taurodeoxycholate, the membrane enzyme binds 10 molecules tightly and approximately 37 molecules in the presence of excess taurodeoxycholate (0.1% solution). The membrane enzyme is identical to the exoenzyme in its reaction with antibodies to exopenicillinase as determined by a radioimmune inhibition assay and immunodiffusion in agar. Heat stability studies indicate a slightly less stable conformation for the membrane enzyme, but this difference largely disappears in the presence of antibody to the exoenzyme. Conversion of membrane enzyme to exoenzyme has been achieved by brief treatment with trypsin, or by incubation of impure preparations at pH 9.0 in 25% potassium phosphate.Since the two forms of penicillinase are very similar in conformation, the hydrophobicity of the membrane form of the enzyme would seem to derive from combination with a hydrophobic moiety, probably phospholipid.     

A solid-phase radioimmunoassay for fibrinogen.

A solid-phase radioimmunoassay for fibrinogen has been developed utilizing [¹⁴C]-methylated fibrinogen as standard antigen and fibrinogen-specific antibodies covalently linked to Sepharose. Fibrinogen was [¹⁴C]-methylated by reductive alkylation using [¹⁴C] formaldehyde and sodium borohydride. The methylated fibrinogen was unaltered in clotting ability and antigenicity.The assay, an isotope dilution assay, is quantitative for picomole amounts of fibrinogen. It is specific for fibrinogen in homologous plasma and in the presence of a variety of other proteins.     

Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands

SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity. Site‐directed spin labeling and electron paramagnetic resonance spectroscopy were used to investigate the surface of interaction on the export chaperone SecB. We examined SecB in complex with the unfolded precursor form of outer membrane protein OmpA as well as with a truncated version of OmpA that includes the transmembrane domain and lacks both the signal peptide and the periplasmic domain. In addition, we studied the binding of SecB to the unfolded mature form of galactose‐binding protein, a soluble periplasmic protein. We have previously used the same strategy to map the binding surface for the precursor of galactose‐binding protein. We show that for all ligands tested the patterns of contact are the same.     

Lactoferrin activates plasma membrane oxidase and Na+/H+ antiport activity.

Lactoferrin is a growth stimulant. The basis for this effect is not clear since it is not thought to be involved in iron uptake through endocytosis. Ferric lactoferrin supports external ferrous chelate formation by K562 and HeLa cells, and ferric lactoferrin stimulates the reduction of external ferric iron by cells. Ferric lactoferrin also stimulates NADH oxidase activity in isolated rat liver plasma membranes and stimulates amiloride sensitive proton release from K562 cells. The evidence that ferric lactoferrin can participate in oxidoreduction reactions at the plasma membrane leading to activation of Na+/H+ exchange provides an alternative explanation for the proliferative effect.     

ROGERSIOMYCES,A NEW GENUS IN THE FILOBASIDIACEAE (HOMOBASIDIOMYCETES) FROM AN AQUATIC HABITAT

Rogersiomyces okefenokeensis gen. et sp. n. is a Homobasidiomycete described in the Filobas-idiaceae. It is characterized by gymnocarpous basidiocarps composed of fasciculate or loose synnematous holobasidia. The basidia are characteristically obclavate with prominent, truncate sterigmata and function as apobasidia. The basidiospores are borne symmetrically, are nonapiculate, and germinate directly to form mycelium or occasionally by repetition. Some examples are presented to illustrate an apparent correlation of apobasidia with an adaptation to aquatic habitats.