BIOMAT Database Logo BIOMAT Database Logo

Increase in cap- and IRES-dependent protein synthesis by overproduction of translation initiation factor eIF4G. 2000

S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba, 263-8522, Japan.

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.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009955 Ornithine Decarboxylase A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine. Ornithine Carboxy-lyase,Carboxy-lyase, Ornithine,Decarboxylase, Ornithine,Ornithine Carboxy lyase
D010448 Peptide Initiation Factors Protein factors uniquely required during the initiation phase of protein synthesis in GENETIC TRANSLATION. Initiation Factors,Initiation Factor,Factors, Peptide Initiation,Initiation Factors, Peptide
D012045 Regulatory Sequences, Nucleic Acid Nucleic acid sequences involved in regulating the expression of genes. Nucleic Acid Regulatory Sequences,Regulatory Regions, Nucleic Acid (Genetics),Region, Regulatory,Regions, Regulatory,Regulator Regions, Nucleic Acid,Regulatory Region,Regulatory Regions
D002455 Cell Division The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION. M Phase,Cell Division Phase,Cell Divisions,Division Phase, Cell,Division, Cell,Divisions, Cell,M Phases,Phase, Cell Division,Phase, M,Phases, M
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012315 RNA Caps Nucleic acid structures found on the 5' end of eukaryotic cellular and viral messenger RNA and some heterogeneous nuclear RNAs. These structures, which are positively charged, protect the above specified RNAs at their termini against attack by phosphatases and other nucleases and promote mRNA function at the level of initiation of translation. Analogs of the RNA caps (RNA CAP ANALOGS), which lack the positive charge, inhibit the initiation of protein synthesis. RNA Cap,5' Capped RNA,5' mRNA Cap Structure,Cap, RNA,Caps, RNA,RNA, 5' Capped

Related Publications

S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Malignant transformation by overproduction of translation initiation factor eIF4G.
November 1997, Cancer research,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Activity of the hepatitis A virus IRES requires association between the cap-binding translation initiation factor (eIF4E) and eIF4G.
September 2001, Journal of virology,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G.
June 1999, Molecular cell,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Characterization of the role of eIF4G in stimulating cap- and IRES-dependent translation in aplysia neurons.
January 2013, PloS one,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation.
September 1995, The Journal of biological chemistry,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation.
August 1997, Proceedings of the National Academy of Sciences of the United States of America,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2.
December 2005, The EMBO journal,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Activation of a GPCR leads to eIF4G phosphorylation at the 5' cap and to IRES-dependent translation.
June 2014, Journal of molecular endocrinology,
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
Interaction of the eIF4G initiation factor with the aphthovirus IRES is essential for internal translation initiation in vivo.
October 2000, RNA (New York, N.Y.),
S Hayashi, and K Nishimura, and T Fukuchi-Shimogori, and K Kashiwagi, and K Igarashi
The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation.
July 2000, Molecular cell,
Copied contents to your clipboard!