| Literature DB >> 10500305 |
Abstract
Initiation of protein synthesis requires both an mRNA and the initiator methionyl (Met)-tRNA to be bound to the ribosome. Most mRNAs are recruited to the ribosome through recognition of the 5' m7G cap by a group of proteins referred to as the cap-binding complex or eIF4F. Evidence is accumulating that eIF4G, the largest subunit of the cap-binding complex, serves as a central adapter by binding to various translation factors and regulators. Other translation factors also have modular structures that facilitate multiple protein-protein interactions, which suggests that adapter functions are common among the translation initiation factors. By linking different regulatory domains to a conserved eIF2-kinase domain, cells adapt to stress and changing growth conditions by altering the translational capacity through phosphorylation of eIF2, which mediates the binding of the initiator Met-tRNA to the ribosome.Entities:
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Year: 1999 PMID: 10500305 DOI: 10.1016/s0968-0004(99)01457-7
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807