Selective accumulation of matrix proteins inside of peroxisomal subdomains

Author:

Ast Julia,Bäcker Nils,Martorana Domenica,Renicke Christian,Stehlik Thorsten,Heimerl Thomas,Taxis ChristofORCID,Bange Gert,Bölker MichaelORCID,Sandrock BjörnORCID,Schink Kay OliverORCID,Freitag JohannesORCID

Abstract

AbstractFormation of specialized reaction spaces prevents interference between distinct cellular pathways. Peroxisomes are cellular compartments involved in a large diversity of metabolic processes. How peroxisomes differentiate into subpopulations and by which mechanism intraorganellar domains are formed remains largely elusive. Here, we report on enzymes from the fungusUstilago maydis, which accumulate inside of peroxisomal subdomains. We describe a short peptide motif (Thr-Ile-Ile-Val) sufficient to trigger focal localization. Mining for proteins with similar motifs uncovered several peroxisomal matrix proteins that accumulate in intraorganellar foci. These foci are enriched in the enzyme urate oxidase – a typical constituent of the paracrystalline core of peroxisomes. Upon peroxisome proliferation uneven distribution of focal structures results in the formation of peroxisome subpopulations with different protein content. The underlying principle of subdomain formation is evolutionary conserved in mammalian peroxisomes and formation of similar foci was also observed inside of mitochondria. We propose that peroxisomal proteins show an individual propensity to self-assemble. This formation of protein aggregates appears to be a ubiquitous driving force to spatially organize the peroxisomal proteome.

Publisher

Cold Spring Harbor Laboratory

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. The peroxisome: an update on mysteries 3.0;Histochemistry and Cell Biology;2024-01-20

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