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82 Poly(A) tail synthesis and regulation: recent structural insights Traci M Tanaka Hall Polyadenylation at the 3′ ends of mRNAs is critical to the 250 nucleotides. PAP is a template-independent polymerase. translation and stability of the messages. Recently determined It belongs to a superfamily of nucleotidyl transferases structures of poly(A) polymerase, U1A and domains of the including mammalian DNA polymerase β and kanamycin poly(A)-binding protein provide a framework for understanding nucleotidyl transferase [4]. These enzymes contain a the synthesis and regulation of the poly(A) tail. conserved catalytic domain that possesses three invariant carboxylate residues essential for the activity of the Addresses enzymes. They catalyze the transfer of a nucleotidyl group Laboratory of Structural Biology, National Institute of Environmental to a free OH group with the release of pyrophosphate. Health Sciences, National Institutes of Health, PO Box 12233, MD F3-05, Research Triangle Park, NC 27709, USA; In addition to the 3′ poly(A) tail, a 5′ 7-methyl-G cap is e-mail: hall4@niehs.nih.gov added to the mRNA. The cap and poly(A) tail act Current Opinion in Structural Biology 2002, 12:82–88 synergistically to stimulate translation [5]. The cap is 0959-440X/02/$ — see front matter recognized by a ternary complex, eIF4F, composed of a © 2002 Elsevier Science Ltd. All rights reserved. cap-binding protein (eIF4E), a helicase (eIF4A) and an