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* * Figure 6-24. The reactions that cap the 5′ end of each RNA molecule synthesized by RNA polymerase II. The final cap contains a novel 5′-to-5′ linkage between the positively charged 7-methyl G residue and the 5′ end of the RNA transcript (see Figure 6-22B). The letter N represents any one of the four ribonucleotides, although the nucleotide that starts an RNA chain is usually a purine (an A or a G). (After A.J. Shatkin, BioEssays 7:275–277, 1987. ? ICSU Press.) * Figure 6-26. The RNA splicing reaction. (A) In the first step, a specific adenine nucleotide in the intron sequence (indicated in red) attacks the 5′ splice site and cuts the sugar-phosphate backbone of the RNA at this point. The cut 5′ end of the intron becomes covalently linked to the adenine nucleotide, as shown in detail in (B), thereby creating a loop in the RNA molecule. The released free 3′-OH end of the exon sequence then reacts with the start of the next exon sequence, joining the two exons together and releasing the intron sequence in the shape of a lariat. The two exon sequences thereby become joined into a continuous coding sequence; the released intron sequence is degraded in due course. * Figure 6-27. Alternative splicing of the α-tropomyosin gene from rat. α-tropomyosin is a coiled-coil protein (see Figure 3-11) that regulates contraction in muscle cells. The primary transcript can be spliced in different ways, as indicated in the figure, to produce distinct mRNAs, which then give rise to variant proteins. Some of the splicing patterns are specific for certain types of cells. For example, the α-tropomyosin made in striated muscle is different from that made from the same gene in smooth muscle. The arrowheads in the top part of the figure demark the sites where cleavage and poly-A addition can occur. * Figure 6-52. A tRNA molecule. In this series of diagrams, the same tRNA molecule—in this case a tRNA specific for the amino acid phenylalanine (Phe)—is depicted in various ways. (A) The cl
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