A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA.

Sonenberg, Nahum; Morgan, M.; Merrick, William C.; Shatkin, Aaron J.

doi:10.1073/pnas.75.10.4843

Cited by 349 publications

(249 citation statements)

References 32 publications

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“…A role for the specific interaction of certain proteins with the cap of mRNA during eukaryotic translation initiation can be suggested on the basis of the present findings and previous observation that mammalian cell initiation factors contain a 24,000 dalton cap-binding protein (5,32). A first step in protein synthesis may be the formation of pre-initiation complexes between the 5'-end of capped mRNA and the 24,000 dalton polypeptide.…”

mentioning

confidence: 60%

“…By contrast, Kaempfer et al (4) showed that the binding of eIF-2 to capped as well as uncapped mRNA was decreased by m CGMP. Our observations indicated that the filter binding technique is unreliable for determining cap-specific interactions because most eukaryotic C) Information Retrieval Limited 1 Falconberg Court London Wl V 5FG England 15 initiation factors tend to adsorb to RNA, including ribosomal species, thus masking the detection of any cap-specific interactions with mRNA (5). Furthermore, cap analogs including m GMP and m GDP can interfere non-specifically with nucleoprotein complex formation at low concentrations of RNA or protein (6).…”

Section: Introductionmentioning

confidence: 82%

“…Hans Trachsel) under conditions described previously (5). The complexes formed between eIF-3 and mRNA were reduced with NaCNBH3 and analyzed by electrophoresis on SDS-polyacrylamide gels and fluorography (5).…”

Section: '3mentioning

confidence: 99%

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Interaction of a limited set of proteins with different mRNAs and protection of 5′-caps against pyrophosphatase digestion in initiation complexes

et al. 1979

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A variety of 5'-3H-methyl-labeled, oxidized viral mRNAs were used as probes for detecting in wheat germ initiation complexes proteins that interact with, and can be cross-linked to, the 5'-cap structure. A limited and reproducible set of specific proteins was obtained with the different mRNAs. The binding of these proteins to the 5'-end of mRNA apparently results in protection against nucleotide pyrophosphatase digestion of the cap even in initiation complexes in which the 5'-end is susceptible to pancreatic RNase digestion. Cross-linked proteins from mammalian initiation complexes comigrated with several of the subunits of similarly treated eIF-3. A model for cap binding protein interaction with mRNA cap during initiation of translation is suggested.

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mentioning

confidence: 60%

Section: Introductionmentioning

confidence: 82%

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Interaction of a limited set of proteins with different mRNAs and protection of 5′-caps against pyrophosphatase digestion in initiation complexes

et al. 1979

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“…The cap-structure is specifically recognized by eukaryotic initiation factor 4F (eIF4F) (Gingras et al, 1999), which contains three initiation factors: 1) eIF4E, the cap-binding factor (Sonenberg et al, 1978); 2) eIF4A, a DEAD box RNA helicase; and 3) eIF4G, a large protein that acts as a scaffold between the ribosome and the mRNA (Imataka et al, 1998). With respect to translation initiation, eIF4E is regulated via phosphorylation and direct interactions with inhibitory eIF4E-binding proteins (4E-BPs).…”

Section: Regulation Of Mtor and Its Effectorsmentioning

confidence: 99%

Altered protein synthesis is a trigger for long-term memory formation

Klann

Sweatt

2008

Neurobiology of Learning and Memory

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SummaryThere is ongoing debate concerning whether new protein synthesis is necessary for, or even contributes to, memory formation and storage. This review summarizes a contemporary model proposing a role for altered protein synthesis in memory formation and its subsequent stabilization. One defining aspect of the model is that altered protein synthesis serves as a trigger for memory consolidation. Thus, we propose that specific alterations in the pattern of neuronal protein translation serve as an initial event in long-term memory formation. These specific alterations in protein readout result in the formation of a protein complex that then serves as a nidus for subsequent perpetuating reinforcement by a positive feedback mechanism. The model proposes this scenario as a minimal but requisite component for long-term memory formation. Our description specifies three aspects of prevailing scenarios for the role of altered protein synthesis in memory that we feel will help clarify what, precisely, is typically proposed as the role for protein translation in memory formation. First, that a relatively short initial time window exists wherein specific alterations in the pattern of proteins translated (not overall protein synthesis) is involved in initializing the engram. Second, that a selfperpetuating positive feedback mechanism maintains the altered pattern of protein expression (synthesis or recruitment) locally. Third, that other than the formation and subsequent perpetuation of the unique initializing proteins, ongoing constitutive protein synthesis is all that is minimally necessary for formation and maintenance of the engram. We feel that a clear delineation of these three principles will assist in interpreting the available experimental data, and propose that the available data are consistent with a role for protein synthesis in memory.

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“…Specific binding of initiation factors to mRNA sequences is thought to play a role in the recognition of messenger and its positioning on the 40 S ribosomal subunit [6][7][8][9][10][11]. In previous studies, the nitrocellulose filter technique was employed to demonstrate the mRNA-binding properties of initiation factors [6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Ultraviolet-crosslinking reveals specific affinity of eukaryotic initiation factors for Semliki Forest virus mRNA

Setyono¹,

Steeg²,

Voorma³

1984

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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Eukaryotic initiation factors (elF) associate readily with 32 P-labeled Semliki Forest virus (SFV) mRNA in vitro, forming complexes which can be crosslinked by 254 nm ultraviolet irradiation. After ribonuclease digestion, the initiation factors were released and analysed by gel electrophoresis. Autoradiography revealed proteins by virtue of crosslinked 32 P-labeled mRNA fragments, elF-4A, -4B and -4C as well as three subunits of elF-3 could be crosslinked with SFV mRNA. None of these proteins bound to ribosomal RNAs.

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A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA.

Cited by 349 publications

References 32 publications

Interaction of a limited set of proteins with different mRNAs and protection of 5′-caps against pyrophosphatase digestion in initiation complexes

Interaction of a limited set of proteins with different mRNAs and protection of 5′-caps against pyrophosphatase digestion in initiation complexes

Altered protein synthesis is a trigger for long-term memory formation

Ultraviolet-crosslinking reveals specific affinity of eukaryotic initiation factors for Semliki Forest virus mRNA

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