Nucleic Acids Research, Vol 27, Issue 10 2181-2188, Copyright © 1999 by Oxford University Press
CR Rodriguez, T Takagi, EJ Cho and S Buratowski
The Saccharomyces cerevisiae mRNA capping enzyme consists of two subunits:
the RNA 5'-triphosphatase (Cet1) and the mRNA guanylyltransferase (Ceg1).
Using computer homology searching, a S. cerevisiae gene was identified that
encodes a protein resembling the C- terminal region of Cet1. Accordingly,
we designated this gene CTL1 (capping enzyme RNAtriphosphatase-like 1).
CTL1 is not essential for cell viability and no genetic or physical
interactions with the capping enzyme genes were observed. The protein is
found in both the nucleus and cytoplasm. Recombinant Ctl1 protein releases
gamma-phosphate from the 5'-end of RNA to produce a diphosphate terminus.
The enzyme is specific for polynucleotide RNA in the presence of magnesium,
but becomes specific for nucleotide triphosphates in the presence of
manganese. Ctl1 is the second member of the yeast RNA triphosphatase
family, but is probably involved in an RNA processing event other than mRNA
capping.
ARTICLES
A Saccharomyces cerevisiae RNA 5'-triphosphatase related to mRNA capping enzyme
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
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