Characterization of Seed Protein Fractions from Castanea spp

Seed proteins of Castanea sativa and C. crenata were extractedby sequential procedures. Albumins accounted for over 20% ofthe total protein. Globulins were the main storage proteinsand represented close to half of the total protein. Additionof 2-mercaptoethanol was essential for maximum extraction ofthe globulins, a fraction with an amino acid composition similarto that of the 1 IS storage protein from legumes. Negligibleamounts of prolamins (<3%) were present in the seeds. Glutelinsrepresented just under 30% of the total protein. The proteinfractions were characterized by electrophoresis in polyacrylamidegels. The glutelin fraction contained unextracted globulinseven when 2-mercaptoethanol was used. Key words: Castanea spp, seeds, storage protein     

Field and experimental evidence of the effect of Jenynsia multidentata, a small omnivorous–planktivorous fish, on the size distribution of zooplankton in subtropical lakes

1. Small cladocerans, copepod nauplii and rotifers often dominate the zooplankton community in tropical and subtropical lakes. This is probably because of high predation pressure by small omnivorous–planktivorous fish, but experimental evidence is scarce.
2. This study used two approaches to test the effect of the small omnivorous–planktivorous fish species Jenynsia multidentata , which is frequently abundant in (sub)tropical eutrophic lakes in South America, on the size distribution of zooplankton. In Lake Blanca (Uruguay), which lacks any piscivores, we sampled seasonally for both fish and zooplankton. We also conducted an outdoor mesocosm experiment with treatments containing or lacking J. multidentata .
3. Together, the empirical and experimental data suggest that J. multidentata predation plays an important role in modulating the size structure of the zooplankton community in subtropical lakes. In the absence of J. multidentata , stocked large-sized zooplankters like Daphnia obtusa were abundant in the experiments, while small-sized zooplankton dominated in the presence of fish, as they did in the lake itself from spring to the end of the season.     

BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites

BNIP3 (formerly NIP3) is a pro-apoptotic, mitochondrial protein classified in the Bcl-2 family based on limited sequence homology to the Bcl-2 homology 3 (BH3) domain and COOH-terminal transmembrane (TM) domain. BNIP3 expressed in yeast and mammalian cells interacts with survival promoting proteins Bcl-2, Bcl-X(L), and CED-9. Typically, the BH3 domain of pro-apoptotic Bcl-2 homologues mediates Bcl-2/Bcl-X(L) heterodimerization and confers pro-apoptotic activity. Deletion mapping of BNIP3 excluded its BH3-like domain and identified the NH(2) terminus (residues 1-49) and TM domain as critical for Bcl-2 heterodimerization, and either region was sufficient for Bcl-X(L) interaction. Additionally, the removal of the BH3-like domain in BNIP3 did not diminish its killing activity. The TM domain of BNIP3 is critical for homodimerization, pro-apoptotic function, and mitochondrial targeting. Several TM domain mutants were found to disrupt SDS-resistant BNIP3 homodimerization but did not interfere with its killing activity or mitochondrial localization. Substitution of the BNIP3 TM domain with that of cytochrome b(5) directed protein expression to nonmitochondrial sites and still promoted apoptosis and heterodimerization with Bcl-2 and Bcl-X(L). We propose that BNIP3 represents a subfamily of Bcl-2-related proteins that functions without a typical BH3 domain to regulate apoptosis from both mitochondrial and nonmitochondrial sites by selective Bcl-2/Bcl-X(L) interactions.