Dataset Information

Ovarian proteomics and ubiquitin-proteomics of Drosophila

ABSTRACT: Ovarian proteomics and ubiquitin-proteomics of Wolbachia-infected and uninfected D. melanogaster

ORGANISM(S): Drosophila Melanogaster

SUBMITTER: Yufeng Wang

PROVIDER: PXD072187 | iProX | Fri Dec 19 00:00:00 GMT 2025

REPOSITORIES: iProX

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Publications

Wolbachia-induced proteostasis remodeling in ovaries supports cytoplasmic incompatibility rescue in Drosophila.

Zhang Hua-Bao HB Zong Qiong Q Naisaierding Pazilanmu P Wang Yu-Feng YF

Journal of insect physiology 20260520

The endosymbiont Wolbachia can modulate host reproduction to promote its own spread through host populations. Cytoplasmic incompatibility (CI) is a prevalent reproductive strategy induced by Wolbachia in insects, wherein embryos from infected males and uninfected females cannot develop normally; however, infected females rescue this embryonic lethality, thereby favoring its maternal transmission. The ovarian mechanisms that facilitate Wolbachia transmission and enable CI rescue remain largely un ...[more]

PMID: 42155847

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Project description:Post-translational control by ubiquitin regulates various aspects of cellular biology. This chemical modification on proteins presents itself in numerous iterations, from a single mono-ubiquitination event to chains of poly-ubiquitin. Among the various types of poly-ubiquitin constructed are untethered species that comprise a series of ubiquitin moieties linked to one another, but free from another protein. The current notion is that these unanchored poly-ubiquitin species are deleterious to the cell and are rapidly deconstructed. We recently examined the toxicity and utilization of untethered poly-ubiquitin in an intact organism by using the fruit fly, Drosophila melanogaster. We found that these ubiquitin species are largely innocuous to flies and that free poly-Ub can be controlled by being degraded by the proteasome or being conjugated onto another protein as a single unit. However, whether the fly is mounting an organismal defense against untethered chains was not explored in detail. Here, we conducted RNA-seq analyses to examine at the transcriptome level the impact of unanchored poly-Ub in the fly. We found ~90 transcripts whose expression is altered in the presence of different types of unanchored poly-ubiquitin. The set of genes identified was mostly devoid of ubiquitin-, proteasome- or autophagy-related components. The largest gene ontology category identified, housing ~15 of the altered genes, was proteolysis. The seeming absence of a large and multipronged response to unanchored ubiquitin chains in the fly supports the conclusion that these species need not be toxic in vivo and underscores the need to reexamine the role of free ubiquitin chains in the cell. We designed two types of poly-Ub chains with six Ub molecules in tandem. They cannot be cleaved by DUBs (there are no "GG" motifs linking the Ub molecules). Ub6-GG can be conjugated in toto onto other proteins; Ub6-Stop cannot. We drove ubiquitous expression using sqh-Gal4, and then performed RNA-Seq on adult flies to determine any cellular response to the presence of our unanchored Ub chains.

Dataset Information

Ovarian proteomics and ubiquitin-proteomics of Drosophila

Publications

Wolbachia-induced proteostasis remodeling in ovaries supports cytoplasmic incompatibility rescue in Drosophila.

Similar Datasets

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