Nucleic Acids Research, 1983, Vol. 11, No. 5 1405-1418
© 1983
ENZYMOLOGY |
RNA 3'-terminal phosphate cyclase activity and RNA ligation in HeLa cell extract
*Institute of Biochemistry and Biophysics, Polish Academy of Sciences 02-532 Warsaw, Poland
Institut für Biochemie, Universität Würzburg D-8700 Wurzburg, FRG
+Roche Institute of Molecular Biology Nutley, NJ 07110, USA
Received December 6, 1982. Revised February 3, 1983. Accepted February 3, 1983.
HeLa cell extract contains RNA ligase activity that converts linear polyribonucleotides to covalently closed circles. RNA substrates containing 2',3'-cyclic phosphate and 5'-hydroxyl termini are circularized by formation of a normal 3',5' phosphodiester bond. This activity differs from a previously described wheat germ RNA ligase which circularizes molecules with 2',3'-cyclic and 5' phosphate ends by a 2'-phosphomonoester, 3',5'-phosphodiester linkage (Konarska et al., Nature 293, 112–116, 1981; Proc. Natl. Acad. Sci. USA 79, 1471–1478, 1982). The HeLa cell ligase can also utilize molecules with 3'-phosphate ends. However, in this case ligation is preceded by an ATP-dependent conversion of the 3'-terminal phosphate to the 2',3' cyclic form by a novel activity, RNA 3'-terminal phosphate cyclase. Both RNA ligase and RNA 3'-terminal phosphate cyclase activities are also present in extract of Xenopus oocyte nuclei, consistent with a role in RNA processing.
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