The polar microbiota
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA588686 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR10912800.fastq.gz | Fastqsanger.gz | |||
| SRR10912900.fastq.gz | Fastqsanger.gz | |||
| SRR10912801.fastq.gz | Fastqsanger.gz | |||
| SRR10912901.fastq.gz | Fastqsanger.gz | |||
| SRR10912802.fastq.gz | Fastqsanger.gz |
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2012-02-01 | E-GEOD-29993 | biostudies-arrayexpress
Project description:Clinicians need additional metrics for predicting quality of human oocytes for IVF procedures. Human polar bodies reflect the oocyte transcript profile. Quantitation of polar body mRNAs could allow for both oocyte ranking and embryo preferences in IVF applications. The transcriptome of a polar body has never been reported, in any organism.
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Project description:The polar filaments and polar tubes of Nosema bombycis were successfully purified by differential centrifugation, and the protein components were identified by proteomic methods, and the functions of these proteins were commented. These results will provide some reference value and significance for future research on the polar tube and infection mechanism of microsporidium.
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Project description:During host cell invasion, microsporidia translocate their entire cytoplasmic contents through a thin, hollow superstructure known as the polar tube. To achieve this, the polar tube transitions from a compact spring-like state inside the environmental spore to a long needle-like tube capable of longrange sporoplasm delivery. The unique mechanical properties of the building blocks of the polar tube allow for an explosive transition from compact to extended state and support the rapid cargo translocation process. The molecular and structural factors enabling this ultrafast process and the ultrastructural changes during cargo delivery remain a mystery. Here, we employ light microscopy and in situ cryo-electron tomography to visualize multiple ultrastructural states of the polar tube, allowing us to evaluate the kinetics of its germination and characterize the underlying morphological transitions. We describe a cargo-filled state with a unique ordered arrangement of microsporidian ribosomes, which cluster along the thin tube wall, and an empty post-translocation state with a reduced diameter but a thicker wall. Together with endogenous compositional information from an affinity-purified polar tube, our work provides comprehensive novel data on the infection apparatus of microsporidia and demonstrates that ribosomes are efficiently transported through polar tubes in a spiral-like parallel arrangement.
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Project description:We have recently shown that the polar transcriptome of E. coli is unique compared to the membrane and cytosolic ones. Several factors were suggested to mediate mRNA localization to the membrane, but the mechanism of localizing mRNAs to the poles is not known. We combined a candidate system approach with high-throughput proteomics to identify factors that mediate polar mRNAs localization. We identified MinD as an essential factor in this process, whose binding to RNAs is indirect. We demonstrate that RNase E, previously shown to interact with MinD, is also required for proper localization of polar mRNAs. Using in silico modeling followed by experimental validation, the membrane-binding site in RNase E was found to mediate binding to MinD. Intriguingly, not only does MinD affect RNase E interaction with the membrane, but it also affects its mode of action and dynamics. Polar accumulation of RNase E in ΔminCDE cells resulted in destabilization and depletion of mRNAs from the poles. Finally, we show that mislocalization of polar mRNAs may prevent polar localization of their protein products. Taken together, MinD and RNase E are assigned novel roles, whereas the interplay between them determines the composition of the polar transcriptome, thus affecting the polar proteome.
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