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• W2510177247 abstract "Robert E. Thach Department of Biology Washington University St. Louis, Missouri 63130 Observations over the past few years suggest that expres- sion of many eukaryotic genes is regulated primarily at the translational level. The mechanisms responsible include phosphotylation of initiation factors, secondary and/or ter- tiary mRNA structures, cap-independent initiation, and re- pressor proteins that mask mRNAs. Several topical exam- ples are discussed here; more detailed information is contained in several recent reviews (Hershey, 1991; Trachsel, 1991). All these novel regulatory mechanisms work by modi- fying the normal process of translational initiation. A model illustrating steps that are thought to limit the initiation rate on most mRNAs is shown (adapted from Lawson et al., 1969; see also Jaramillo et al., 1991). Although speculative at some points, this elF-4F pathway summarizes current thinking. The first step in the pathway is an interaction between the mRNA cap and a 25 kd cap recognition protein (~25, also known as elF-4E or CBP I). This protein is either al- ready, or subsequently becomes, associated with two other subunits, elF-4A (~44) and a 220 kd protein (~220) of unknown function. The cytoplasmic concentration of active elF-4E is thought to be less than the sum of the mRNAs; therefore, mRNAs compete with one another in binding to elF-4F. When elF-4E is overproduced, cell transformation results, and phosphorylation of a single serine residue is required for this activity (Lazaris-Karatzas et al., 1990; DeBenedetti and Rhoads, 1990; Morley et al., 1991). The cap recognition step is one of several that ordinarily work in combination to limit the overall rate of mRNA translation. Cap recognition is thought to be hin- dered in several cases by simple steric accessibility, which can be governed either by proteins bound to the mRNA or by mRNA tertiary structure. The next step is helix unwinding, which probably driven bythe ATP-dependent binding of theelF4Asubunit to the first 15 nucleotides of mRNA. elF-4B can enhance the rate of this step. This reaction is prototypical for a large number of RNA helicases (Koonin, 1991). The helix unwinding step can be rate limiting for translation if the RNA-binding site is masked by stable secondary structure. elF-4B then triggers the expulsion of the elF-4E and ~220 subunits of the elF-4F complex from mRNA. The re- leased components can recruit free elF-4A to reconstitute active elF-4F. It is not known for certain whether the origi- nal elF-4A subunit and the elF46 remain bound to mRNA, as suggested by the model; in any event, these two factors can participate in the further unwinding of mRNA secondary (and tertiary) structure. This further unwinding can also be inhibited by mRNA secondary structure, al- though this step is much less structure sensitive than the first helix unwinding step. At some unknown point in the elF-4F pathway, the 435 ribosomal complex also binds and proceeds to scan the mRNA for an AUG codon. This process can also be rate limiting for translation. Rate con- stants have been estimated for the steps described here, and have been incorporated into a kinetic model of protein synthesis called the competition/discrimination model. Two recent observations have refocused interest on these reactions. The first the demonstration that adeno-" @default.
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• W2510177247 date "1992-01-01" @default.
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• W2510177247 title "Cap Recap: The Involvement of elF-4F in Regulating Gene Expression Minireview" @default.
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