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Knockdown of EIF3G inhibits the intracellular protein translation of H1299 cells

ABSTRACT: Knockdown of EIF3G inhibits the intracellular protein translation of H1299 cells

PROVIDER: PRJNA980089 | ENA |

REPOSITORIES: ENA

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Knockdown of EIF3G inhibits the intracellular protein translation of H1299 cells

Project description:eIF3 is the largest translation initiation factor in mammalian cells, consisting of 13 subunits. This translation initiation factor is involved in multiple processes of protein translation in cells, including translation initiation, termination, and ribosome recycling. Several studies have reported that multiple subunits of eIF3 exhibit abnormal expression in tumor cells and play an important role in the occurrence and development of tumors. In this study, it was found that changes in the expression level of EIF3G significantly affected the growth of non-small cell lung cancer. Knockdown of EIF3G inhibited the intracellular protein translation process of non-small cell lung cancer cells H1299. Through the study of translatome, it was found that knockdown of EIF3G significantly affected the cell cycle processes in H1299 cells. In vitro cell experiments also showed that changes in the expression level of EIF3G influences the cell cycle distribution of H1299 cells. This study is the first to explore the impact of knockdown of EIF3G on the translatome of H1299 cells.

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Translatome of A549, H1299 and HBE cells

Project description:We performed translatome and transcriptome sequencing of A549, H1299 and HBE cells and analyzed the translation ratio (TR) of all genes Total RNA and ribosome-bound RNA were extracted from A549, H1299 and HBE cells, and the polyA+ mRNA was sequenced using Illumina GAIIx and HiSeq-2000. The reads were mapped to RefSeq RNA reference sequences and the expression level were quantified by rpkM calculation.

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Glucose depletion inhibits translation initiation in yeast - transcription profiling

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Project description:This is a polysome/monosome profiling study on yeast undergoing glucose depletion. Polysomes and monosomes are extracted and the transcripts bound to each fraction are measured by microarray. The study reveals that glucose depletion inhibits translation initiation in a mechanism involving eIF4A loss and 48S pre-initiation complex accumulation, while the pentose phosphate pathway is co-ordinately up-regulated

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