Abstract
In eukaryotes, stalled and collided ribosomes are recognized by several conserved multicomponent systems, which either block protein synthesis in situ and resolve the collision locally, or trigger a general stress response. Yeast ribosome-binding GTPases RBG1 (DRG1 in mammals) and RBG2 (DRG2) form two distinct heterodimers with TMA46 (DFRP1) and GIR2 (DFRP2), respectively, both involved in mRNA translation. Accumulated evidence suggests that the dimers play partially redundant roles in elongation processivity and resolution of ribosome stalling and collision events, as well as in the regulation of GCN1-mediated signaling involved in ribosome-associated quality control (RQC). They also genetically interact with SLH1 (ASCC3) helicase, a key component of RQC trigger (RQT) complex disassembling collided ribosomes. Here, we present RNA-Seq and ribosome profiling (Ribo-Seq) data from S. cerevisiae strains with individual deletions of the TMA46 and GIR2 genes. Raw RNA-Seq and Ribo-Seq data as well as gene-level readcounts are available in NCBI Gene Expression Omnibus (GEO) repository under GEO accession GSE185458 and GSE185286.
Highlights
We present Ribo-Seq and RNA-Seq data for S. cerevisiae strains lacking translation-associated proteins Tma[46] and Gir[2], as well as for the wild type BY4742 parent strain
The RBG2 (DRG2) containing dimers are not bound to ribosomes under normal conditions.[3,6]. They are clearly related to translation, as GIR2 interacts with the ribosome-bound GCN1, and RBG2GIR2 is responsible for efficient cell growth under amino acid starvation.[5,8]
These results suggest that GIR2 is a physical linker between RBG2 and GCN1 and that this interaction could prevent excessive activation of the GCN2 pathway upon incidental ribosome stalling
Summary
We present Ribo-Seq and RNA-Seq data for S. cerevisiae strains lacking translation-associated proteins Tma[46] and Gir[2], as well as for the wild type BY4742 parent strain. Raw sequencing data are available online in the NCBI Gene Expression Omnibus (GEO accession: GSE185458 and GSE185286)
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