Pathogens of plants and animals produce effector proteins that are transferred into the cytoplasm of host cells to suppress host defenses. One type of plant pathogens, oomycetes, produces effector proteins with N-terminal RXLR and dEER motifs that enable entry into host cells. We show here that effectors of another pathogen type, fungi, contain functional variants of the RXLR motif, and that the oomycete and fungal RXLR motifs enable binding to the phospholipid, phosphatidylinositol-3-phosphate (PI3P). We find that PI3P is abundant on the outer surface of plant cell plasma membranes and, furthermore, on some animal cells. All effectors could also enter human cells, suggesting that PI3P-mediated effector entry may be very widespread in plant, animal and human pathogenesis. Entry into both plant and animal cells involves lipid raft-mediated endocytosis. Blocking PI3P binding inhibited effector entry, suggesting new therapeutic avenues.

In preparing the figures for this article for publication, we inadvertently assembled duplicated images of three panels in Figure 2 (Figure 2O, panel 2 was a duplicate of Figure 2N, panel 2; Figure 2R, panel 2 was a duplicate of Figure 2Q, panel 2; and Figure 2N, panel 3 was a duplicate of Figure 2K, panel 3). Also, in Figure S4, the leaf pictured in panel 8 of Figure S4A was mistakenly a picture of the same leaf as shown in panel 6. In the first two cases, the figures were correct in the original reviewed submission, and the errors occurred in revising the paper for resubmission. Corrected Figures 2 and S4 are shown below. The new figures do not alter any of the conclusions of the study. Finally, in the Experimental Procedures, under Lipid Filter-Binding Assays, the statement, ''Lipids were dissolved in DMSO then spotted .'' should read ''Lipids were dissolved in chloroform: methanol: water (65:30:8) then spotted .''The authors regret any confusion these errors may have caused. All errors have been corrected in the online version of the manuscript.

As Arctic temperatures rise at twice the global rate, sea ice is diminishing more quickly than models can predict. Processes that dictate Arctic cloud formation and impacts on the atmospheric energy budget are poorly understood, yet crucial for evaluating the rapidly changing Arctic. In parallel, warmer temperatures afford conditions favorable for productivity of microorganisms that can effectively serve as ice nucleating particles (INPs). Yet the sources of marine biologically derived INPs remain largely unknown due to limited observations. Here we show, for the first time, how biologically derived INPs were likely transported hundreds of kilometers from deep Bering Strait waters and upwelled to the Arctic Ocean surface to become airborne, a process dependent upon a summertime phytoplankton bloom, bacterial respiration, ocean dynamics, and wind‐driven mixing. Given projected enhancement in marine productivity, combined oceanic and atmospheric transport mechanisms may play a crucial role in provision of INPs from blooms to the Arctic atmosphere.

Phytase, an enzyme that degrades the phosphorus storage compound phytate, has the potential to enhance phosphorus availability in animal diets when engineered into soybean (Glycine max) seeds. The phytase gene from Aspergillus niger was inserted into soybean transformation plasmids under control of constitutive and seed-specific promoters, with and without a plant signal sequence. Suspension cultures were used to confirm phytase expression in soybean cells. Phytase mRNA was observed in cultures containing constitutively expressed constructs. Phytase activity was detected in the culture medium from transformants that received constructs containing the plant signal sequence, confirming expectations that the protein would follow the default secretory pathway. Secretion also facilitated characterization of the biochemical properties of recombinant phytase. Soybean-synthesized phytase had a lower molecular mass than did the fungal enzyme. However, deglycosylation of the recombinant and fungal phytase yielded polypeptides of identical molecular mass (49 kD). Temperature and pH optima of the recombinant phytase were indistinguishable from the commercially available fungal phytase. Thermal inactivation studies of the recombinant phytase suggested that the additional protein stability would be required to withstand the elevated temperatures involved in soybean processing.

Background: High throughput methods, such as high density oligonucleotide microarray measurements of mRNA levels, are popular and critical to genome scale analysis and systems biology. However understanding the results of these analyses and in particular understanding the very wide range of levels of transcriptional changes observed is still a significant challenge. Many researchers still use an arbitrary cut off such as two-fold in order to identify changes that may be biologically significant. We have used a very large-scale microarray experiment involving 72 biological replicates to analyze the response of soybean plants to infection by the pathogen Phytophthora sojae and to analyze transcriptional modulation as a result of genotypic variation.