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Transcription analysis of yeast strains under oxidative stress

ABSTRACT: Transcription analysis of yeast strains under ER stress

PROVIDER: PRJEB71583 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR12391717_1.fastq.gz	Fastqsanger.gz
	ERR12391717_2.fastq.gz	Fastqsanger.gz
	ERR12391718_1.fastq.gz	Fastqsanger.gz
	ERR12391718_2.fastq.gz	Fastqsanger.gz
	ERR12391719_1.fastq.gz	Fastqsanger.gz

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Project description:The accumulation of misfolded proteins in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR), which acts through various mechanisms to reduce ER stress. We previously found ER stress induced by tunicamycin (TM) treatment promotes the activation of small GTPase Arl1 and thereby increasing the recruitment of downstream effector golgin Imh1 to the late-Golgi. However, the role of Imh1 under ER stress remains unknown. In this study, we found Imh1 is required for the recycling of two SNAREs, Snc1 and Tlg1, upon TM-induced ER stress and phosphorylation of Imh1 is required for this regulation. Since Ire1 is the sensor of UPR in yeast and we previous found that Ire1 is required for Arl1-Imh1 activation, we wonder whether Ire1 signaling is also responsible for the TM-induced phosphorylation of Imh1 and the subsequent SNARE transport. We compared the phosphorylation signal of Imh1 in WT with that in the absence of Ire1 and further performed SILAC method in a label swap replication. Collectively, this study illustrates the mechanism of how signaling under ER stress promotes Imh1 in cooperation with another tether factor in regulating the SNARE transport to alleviate ER stress in yeast cells.

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Project description:The yeast genome contains a substantial amount of duplicated ribosomal protein genes. Functional characterization of deletion strains of individual paralogs show that the phenotypes upon deletion are not the same for a given paralog pair, suggesting that ribosomal protein paralog genes have distinct functions and thus are not redundant. Here we aimed to explore the differential function of RPL22A and RPL22B in protein synthesis. For this aim, we compared the ribosome-bound mRNAs found in different polysomal fractions: monosome, polysomal low (2-3ribosomes/mRNA), and polysomal high (>3ribosomes/mRNA), relative to total mRNA, for 3 different yeast strains: ∆RPL22A, ∆RPL22B and wild-type. Our results show that the use of one or the other specific ribosomal paralog affects the protein synthesis rates of specific transcripts, suggesting that each ribosomal protein paralog is optimized for decoding a subset of transcripts. We also find that the ratio of these paralogs changes upon oxidative stress, and propose that ribosome heterogeneity might be employed as a strategy to tune protein translation upon oxidative stress.

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