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Morrison, E.

Publications and source records attributed to Morrison, E..

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Physiological adaptations of leaf litter microbial communities to long-term drought

Drought represents a significant stress to soil microorganisms and is known to reduce microbial activity and organic matter decomposition in Mediterranean ecosystems. However, we still lack a detailed understanding of the drought stress adaptations of microbial decomposers. We hypothesised that drought causes greater microbial allocation to stress tolerance relative to growth pathways. Here we present metatranscriptomic and metabolomic data on the physiological response of in situ microbial communities on plant leaf litter to long-term drought and pulse wetting in Californian grass and shrub ecosystems. Wetting litter after a long dry summer caused only subtle shifts in gene expression. On grass litter, communities from the decade-long ambient and reduced precipitation treatments had distinct functional profiles. The most discernable physiological adaptations to drought were production or uptake of compatible solutes to maintain cellular osmotic balance, and synthesis of capsular and extracellular polymeric substances as a mechanism to retain water. The results show a clear functional response to drought in grass litter communities with greater allocation to survival relative to growth that could affect decomposition under drought. In contrast, communities on chemically more diverse and complex shrub litter had smaller physiological differences in response to long-term drought but higher investment in resource acquisition traits across treatments, suggesting that the functional response to drought is constrained by substrate quality. Our findings suggest, for the first time in a field setting, a trade-off between microbial drought stress tolerance, resource acquisition and growth traits in leaf litter microbial communities.

microbiology

The conserved metalloprotease invadolysin is present in invertebrate haemolymph and vertebrate blood

We identified invadolysin, a novel essential metalloprotease, for functions in chromosome structure, cell proliferation and migration. Invadolysin also plays an important metabolic role in insulin signaling and is the only protease known to localise to lipid droplets, the main lipid storage organelle in the cell. In silico examination of the protein sequence of invadolysin predicts not only protease and lipase catalytic motifs, but also post-translational modifications and the secretion of invadolysin. Here we show that the protease motif of invadolysin is important for its role in lipid accumulation, but not in glycogen accumulation. The lipase motif does not appear to be functionally important for accumulation of lipids or glycogen. Post-translational modifications likely contribute to modulating the level, localisation or activity of invadolysin. We identified a secreted form of invadolysin in the soluble fraction of invertebrate hemolymph (where we observe sexually dimorphic forms) and also vertebrate plasma, including in the extracellular vesicle fraction. Biochemical analysis for various post-translational modifications demonstrated that secreted invadolysin is both N-and O-glycosylated, but not apparently GPI-linked. The discovery of invadolysin in the extracellular milieu suggests a role for invadolysin in normal organismal physiology.\n\nSummary StatementIn this study, we show that the conserved metalloprotease invadolysin is present in invertebrate hemolymph and vertebrate blood, suggesting the protein may function in organismal physiology.

cell biology