ArticleScientific reports2019
HspX promotes the polar localization of mycobacterial protein aggregates.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Article
- Ribosomal RNA methylation by GidB modulates discrimination of mischarged tRNA.bioRxiv : the preprint server for biology · 2026Article
- Mycobacterial nucleoid-associated protein Lsr2 is required for productive mycobacteriophage infection.Nature microbiology · 2023Article
- Arginine methylation sites on SepIVA help balance elongation and septation in Mycobacterium smegmatis.Molecular microbiology · 2023Article
- Selective translation by alternative bacterial ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Forward Genetics Reveals aFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Misfolding of translated proteins occurs in all domains of life. In most cells, misfolded proteins coalesce in discrete aggregates at distinct cellular locations. In many bacteria, including mycobacteria, protein aggregates are located at the cellular pole. Yet the mechanism by which aggregates are sorted to the mycobacterial pole is not known. Here, we show that in Mycobacterium smegmatis, the small heat shock protein HspX plays a critical role in the polar localization of aggregates of a model fluorescent misfolded protein, GLR103. HspX itself has a polar localization, which is dependent on its N-terminal domain. In a strain deleted for hspX, GLR103 is less liable to aggregation and no longer localizes to the pole, and redirecting HspX to the septum radically disrupts the normal polar localization of GLR103 aggregates. To further investigate the role of HspX in native protein aggregation, we performed semi-quantitative mass-spectrometry of mycobacterial protein aggregates in wild-type, hspX-deleted and hspX-overexpressing strains. We identified a subset of proteins that appeared to be HspX-dependent for aggregate formation. Furthermore, we demonstrate that for validated native protein aggregates, sorting to the cellular pole following proteotoxic stress required HspX. In summary, we have identified the cellular function of HspX in Mycobacterium smegmatis as both a pro-aggregase and polar sortase.
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