The Effect of Climate Variability on Gray Whales (Eschrichtius robustus) within Their Wintering Areas

The environmental conditions of the breeding and feeding grounds of the gray whale (Eschrichtius robustus) fluctuates at inter-annual scales in response to regional and basin climate patterns. Thus, the goals of this study were to assess if there are any relationships between summer sea ice on their feeding ground and counts of gray whale mother-calf (MC) pairs at Ojo de Liebre Lagoon (OLL); and if El Niño Southern Oscillation (ENSO) influences the winter distribution of gray whales MC pairs in the three primary breeding lagoons of OLL, San Ignacio Lagoon (SIL) and Santo Domingo Channel north of Bahia Magdalena (SDCh). Maximum February counts of MC pairs were compared with the length of the open-water season at the Bering Sea during the previous year. Then, an ENSO index and sea surface temperature anomalies outside the primary lagoons was compared with the maximum February counts of MC pairs at these lagoons. Results showed that maximum counts of MC pairs in OLL correlates with sea ice conditions in their feeding grounds from the previous feeding season, and this relationship can be attributed to changes in nutritive condition of females. ENSO-related variability influences distribution of MC pairs in the southern area of SDCh during the warm 1998 El Niño and cold 1999 La Niña. This supports the hypothesis that changes in the whales’ distribution related to sea temperature occurs to reduce thermal-stress and optimize energy utilization for newborn whales. Although this last conclusion should be considered in view of the limited data available from all the whales’ wintering locations in all the years considered.     

Variance partitioning of deconstructed periphyton communities: does the use of biological traits matter?

The use of species traits offers a promising approach to the understanding of the main processes underlying metacommunity patterns. We analyzed samples of periphytic algae in 30 environments of the Upper Paraná River floodplain in southeastern Brazil, to test the hypotheses that variation in species composition of algal groups with low dispersal abilities would be mainly explained by spatial variables; on the other hand, algal groups with higher dispersal abilities would be better explained by environmental variables. The variation in community structure was mainly correlated with environmental variables. This result is in line with a growing body of evidence indicating a predominant role of species-sorting processes. The more-refined prediction that the spatial variables would gradually become more important across a gradient of adherence or size was, however, not supported by our analyses. Also, the large unexplained variation suggested that these periphytic communities were assembled by idiosyncratic events, or that other variables that are often neglected in studies of aquatic metacommunities needed to be included.     

eIF2 kinases mediate β-lapachone toxicity in yeast and human cancer cells

β-lapachone (β-lap) is a novel anticancer agent that selectively induces cell death in human cancer cells, by activation of the NQO1 NAD(P)H dehydrogenase and radical oxygen species (ROS) generation. We characterized the gene expression profile of budding yeast cells treated with β-lap using cDNA microarrays. Genes involved in tolerance to oxidative stress were differentially expressed in β-lap treated cells. β-lap treatment generated reactive oxygen species (ROS), which were efficiently blocked by dicoumarol, an inhibitor of NADH dehydrogenases. A yeast mutant in the mitocondrial NADH dehydrogenase Nde2p was found to be resistant to β-lap treatment, despite inducing ROS production in a WT manner. Most interestingly, DNA damage responses triggered by β-lap were abolished in the nde2Δ mutant. Amino acid biosynthesis genes were also induced in β-lap treated cells, suggesting that β-lap exposure somehow triggered the General Control of Nutrients (GCN) pathway. Accordingly, β-lap treatment increased phosphorylation of eIF2α subunit in a manner dependent on the Gcn2p kinase. eIF2α phosphorylation required Gcn1p, Gcn20p and Nde2p. Gcn2p was also required for cell survival upon exposure to β-lap and to elicit checkpoint responses. Remarkably, β-lap treatment increased phosphorylation of eIF2α in breast tumor cells, in a manner dependent on the Nde2p ortholog AIF, and the eIF2 kinase PERK. These findings uncover a new target pathway of β-lap in yeast and human cells and highlight a previously unknown functional connection between Nde2p, Gcn2p and DNA damage responses.     

DMAP-85: A τ-Like Protein from Drosophila melanogaster Larvae

Abstract: Microtubule-associated proteins (MAPs) play major regulatory roles in the organization and integrity of the cytoskeletal network. Our main interest in this study was the identification and the analysis of structural and functional aspects of Drosophila melanogaster MAPs. A novel MAP with a relative molecular mass of 85 kDa from Drosophila larvae was found associated with taxol-polymerized microtubules. In addition, this protein bound to mammalian tubulin in an overlay assay and coassembled with purified bovine brain tubulin in microtubule sedimentation experiments. The estimated stoichiometry of 85-kDa protein versus tubulin in the polymers was 1:5.3 ± 0.2 mol/mol. It was shown that the 85-kDa protein bound specifically to an affinity column of Sepharose-βII-(422–434) tubulin peptide, which contains the sequence of the MAP binding domain on βII-tubulin. Affinity-purified 85-kDa protein enhanced microtubule assembly in a concentration-dependent manner. This effect was significantly decreased by the presence of the βII-(422–434) peptide in the assembly assays, thus confirming the specificity of the 85-kDa protein interaction with the C-terminal domain on tubulin. Furthermore, this protein also exhibited a strong affinity for calmodulin, based on affinity chromatographic assays. Monoclonal and polyclonal anti-τ antibodies, including sequence-specific probes that recognize repeated microtubule-binding motifs on τ, MAP-2, and MAP-4 and specific N-terminal sequences of τ, cross-reacted with the 85-kDa protein from Drosophila larvae. These results suggest that τ and Drosophila 85-kDa protein share common functional and structural epitopes. We have named this protein as DMAP-85 for Drosophila MAP. The finding on a Drosophila protein with functional homology and structural similarities to mammalian τ opens new perspectives to understand the cellular roles of MAPs.     

Assessment of different systems for the production of aldonic acids and sorbitol by calcium alginate-immobilized Zymomonas mobilis cells

Bioprocess and Biosystems Engineering - Equimolar amounts of lactobionic acid and sorbitol may be obtained in a reaction catalyzed by the enzymes glucose–fructose oxidoreductase and...     

Identification of potential allosteric binding sites in cathepsin K based on intramolecular communication

Network theory methods and molecular dynamics (MD) simulations are accepted tools to study allosteric regulation. Indeed, dynamic networks built upon correlation analysis of MD trajectories provide detailed information about communication paths between distant sites. In this context, we aimed to understand whether the efficiency of intramolecular communication could be used to predict the allosteric potential of a given site. To this end, we performed MD simulations and network theory analyses in cathepsin K (catK), whose allosteric sites are well defined. To obtain a quantitative measure of the efficiency of communication, we designed a new protocol that enables the comparison between properties related to ensembles of communication paths obtained from different sites. Further, we applied our strategy to evaluate the allosteric potential of different catK cavities not yet considered for drug design. Our predictions of the allosteric potential based on intramolecular communication correlate well with previous catK experimental and theoretical data. We also discuss the possibility of applying our approach to other proteins from the same family.