C. elegans (strain SS104, sterile mutant) Control vs. NAC RNAi
Ontology highlight
ABSTRACT:
ORGANISM(S): Caenorhabditis elegans
PROVIDER: GSE63928 | GEO | 2015/02/12
SECONDARY ACCESSION(S): PRJNA269611
REPOSITORIES: GEO
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Project description:mRNA translation is a highly dynamic process that has been shown to modulate cell adaptation to stress conditions. Upon ribosome impairment, ZAKα affects the metabolic profile of intestinal cells, however the mechanism by which this is promoted is still unclear. Here, we identified the nascent polypeptide-associated complex (NAC) as a central player in the metabolic regulation triggered by ribosome impairment. Furthermore, we show that NAC is essential for the survival of the highly oxidative phosphorylation (OXPHOS) reliant intestinal stem cells (ISCs), being translationally regulated itself. NAC interacts with the ribosome and promotes the transport of the translation machinery and newly-formed peptides to the proximity of the mitochondria, allowing the import of proteins essential for processes such as OXPHOS. Upon translation stress, NAC is inhibited through an interaction with ZAKα, leading to the downregulation of OXPHOS. Overall, our findings unveil that NAC is a central player in translation-mediated metabolic regulation in intestinal cells.
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Project description:In this study, NAC was UV-crosslinked using the photo-crosslinking amino acid p-benzoyl-L-phenylalanine (pBPA) in order to determine specific interaction sites of the alphaNAC N-terminus in the native protein structure. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-XL-MS) was used to compare crosslink abundances of a NAC mutant versus wild type NAC in order to determine the influence of the mutated motive on the structural dynamics of NAC.
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Project description:To understand the orientation of Hsp70 Ssb on the ribosome in living Saccharomyces cerevisiae cells we incorporated the noncanonical, photoactivatable amino acid p-benzoyl-L-phenylalanine (Bpa) in place of specific individual endogenous amino acids in Ssb1. To identify the proteins to which Ssb1Bpa crosslinked we performed mass spectrometry. The results revealed that Bpa incorporated at the tip of the “lid” subdomain cross linked to the nascent chain associated complex (NAC), while Bpa incorporated into further down the lid crosslinked to ribosomal protein uL29.
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Project description:C. elegans (strain SS104, sterile mutant) Control vs. NAC RNAi
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Project description:All animals must maintain genome and proteome integrity, especially when experiencing endogenous or exogenous stress. To cope, organisms have evolved sophisticated and conserved response systems: unfolded protein responses (UPRs) ensure proteostasis while the DNA damage response (DDR) maintains genome integrity. Emerging evidence suggests that UPRs and DDRs crosstalk, but the extent of crosstalk remains poorly understood. Here, we demonstrate that inactivation of the DNA primases pri-1 and pri-2, which synthesize RNA primers at replication forks and whose inactivation causes DNA damage, activates the UPR of the endoplasmic reticulum (UPR-ER) in Caenorhabditis elegans, with especially strong activation in the germline. We observed activation of both the inositol-requiring-enzyme 1 (ire-1) and the protein kinase RNA-like ER kinase (PEK-1) branches of the UPR-ER. Interestingly, activation of the UPR-ER output gene hsp-4/BiP was partially independent of its canonical activators, ire-1 and xbp-1, and instead required the third branch of the UPR-ER, atf-6, suggesting functional redundancy. We further found that primase depletion specifically induces the UPR-ER, but not the mechanistically distinct cytosolic or mitochondrial UPRs, suggesting that primase inactivation causes compartment-specific rather than global stress. Functionally, loss of ire-1 or pek-1 sensitized animals to replication stress caused by hydroxyurea. Finally, transcriptome analysis of pri-1 embryos revealed several deregulated processes that could cause UPR-ER activation, including protein glycosylation, calcium signaling, and fatty acid desaturation. Together, our data show that the UPR-ER, but not other UPRs, responds to replication fork stress and that the UPR-ER is required to alleviate this stress.
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