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Science 25 August 2000:
Vol. 289. no. 5483, pp. 1346 - 1349
DOI: 10.1126/science.289.5483.1346
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Reports
Structure of Yeast Poly(A) Polymerase Alone and in Complex with 3'-dATP
Joel Bard,1
Alexander M. Zhelkovsky,2
Steffen Helmling,2
Thomas N. Earnest,3
Claire L. Moore,2
Andrew Bohm14*
Polyadenylate [poly(A)] polymerase (PAP) catalyzes the
addition of a polyadenosine tail to almost all eukaryotic
messenger RNAs (mRNAs). The crystal structure of the PAP from
Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine
triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is
composed of three domains that encircle the active site. The
arrangement of these domains, however, is quite different from that
seen in polymerases that use a template to select and position their
incoming nucleotides. The first two domains are functionally analogous
to polymerase palm and fingers domains. The third domain is attached to
the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are
bound to Pap1. One occupies the position of the incoming base, prior to
its addition to the mRNA chain. The other is believed to occupy the
position of the 3' end of the mRNA primer.
1 Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
2 Tufts
University School of Medicine, Department of Molecular Microbiology,
Boston, MA 02111, USA.
3 Macromolecular
Crystallography Facility at the Advanced Light Source (ALS), Physical
Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley,
CA 94720, USA.
4 Tufts University School of
Medicine, Department of Biochemistry, Boston, MA 02111, USA.
*
To whom correspondence should be addressed. E-mail:
bohm{at}bbri.org
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