AI Article Synopsis

  • The study investigates how proteins involved in DNA repair and cellular stress responses change their location in the cell during genotoxic stress, focusing on the splicing factor Hsh155.
  • Hsh155 moves away from its usual partners and accumulates in specific protein quality control aggregates in both the nucleus and cytoplasm when exposed to alkylation stress, a process influenced by molecular chaperones and TORC1 signaling.
  • This relocalization of Hsh155 is linked to changes in gene expression, including increased intron retention and reduced splicing efficiency, ultimately aiding the cell's recovery from stress.

Article Abstract

Upon genotoxic stress, dynamic relocalization events control DNA repair as well as alterations of the transcriptome and proteome, enabling stress recovery. How these events may influence one another is only partly known. Beginning with a cytological screen of genome stability proteins, we find that the splicing factor Hsh155 disassembles from its partners and localizes to both intranuclear and cytoplasmic protein quality control (PQC) aggregates under alkylation stress. Aggregate sequestration of Hsh155 occurs at nuclear and then cytoplasmic sites in a manner that is regulated by molecular chaperones and requires TORC1 activity signaling through the Sfp1 transcription factor. This dynamic behavior is associated with intron retention in ribosomal protein gene transcripts, a decrease in splicing efficiency, and more rapid recovery from stress. Collectively, our analyses suggest a model in which some proteins evicted from chromatin and undergoing transcriptional remodeling during stress are targeted to PQC sites to influence gene expression changes and facilitate stress recovery.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5716266PMC
http://dx.doi.org/10.1083/jcb.201612018DOI Listing

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