In the course of protein biosynthesis, the 3'-ends of aminoacyl-tRNA (aa-tRNA) and peptidyl-t RNA specifically interact with macromolecules of the protein biosynthesis machinery. The 3'-end of tRNA consists of an invariant C-C-A single strand. Interaction of the aminoacyl-tRNA 3'-end with elongation factor Tu (EF-Tu) containing bound GTP is necessary for the formation of the aa-tRNA. EF-TU . GTP complex and, after the complex binds to the ribosome, for the GTP hydrolysis. This process is followed by the specific binding of the aminoacyl-tRNA 3'-end to the aminoacyl (A) site of the ribosome. In this review, a model is proposed that involves Watson-Crick base pairing of the C-C sequence of the aminoacyltRNA 3'-end with a specific G-G sequence of the ribosomal 23s RNA. Similarly, peptidyltRNA binds with its 3'-end to the peptidyl (P) site of the ribosome. This binding may also involve Watson-Crick base pairing of the C-C-A sequence with a complementary sequence of 23s RNA. It is proposed that peptide bond formation is catalyzed by a functional site of the 23s RNA located near the 3'-ends of aminoacyl-tRNA and peptidyl-tRNA. A model is suggested in which two loops of the 23s RNA, brought into close proximity via folding, are involved both in binding the 3'-ends of the tRNAs and in catalyzing peptide bond formation. This model presumes a dynamic structure for ribosomal RNA, which is modulated by interaction with elongation factors and ribosomal proteins.