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• W2022235281 endingPage "123" @default.
• W2022235281 startingPage "117" @default.
• W2022235281 abstract "The role of eIF4G during the initiation of protein synthesis was studied using mouse mammary carcinoma FM3A cells and FM4G cells that overproduce an N-terminally truncated form of eIF4G, which lacks the binding site of poly(A)-binding protein. An increase in eIF4G was correlated with an increase in protein synthesis and RNA helicase activity. Translation of mRNAshaving both short and long 5'-untranslated regions (5'-UTR) increased significantly in FM4G cells compared to that in FM3A cells. Both full-length and N-terminally truncated eIF4G transfectants of NIH3T3 cells formed colonies in soft agar and increased the saturation density of cell growth, indicating that both eIF4Gs function similarly. We also found that an internal ribosome entry site (IRES) exists in the 5'-UTR of ornithinedecarboxylase mRNA and that IRES-dependent protein synthesis increased in FM4G cells. Our results indicate that an increase in eIF4G contributes to the formation of active eIF4F similarly to that caused by an increase in eIF4E, as well as to a stimulation of IRES-dependent protein synthesis." @default.
• W2022235281 created "2016-06-24" @default.
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• W2022235281 date "2000-10-01" @default.
• W2022235281 modified "2023-10-17" @default.
• W2022235281 title "Increase in Cap- and IRES-Dependent Protein Synthesis by Overproduction of Translation Initiation Factor eIF4G" @default.
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• W2022235281 doi "https://doi.org/10.1006/bbrc.2000.3637" @default.
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