Nucleic Acids Research, Vol 27, Issue 24 4671-4678, Copyright © 1999 by Oxford University Press
CK Ho, K Lehman and S Shuman
Saccharomyces cerevisiae RNA triphosphatase (Cet1p) and RNA
guanylyltransferase (Ceg1p) interact in vivo and in vitro to form a
bifunctional mRNA capping enzyme complex. Cet1p binding to Ceg1p stimulates
the guanylyltransferase activity of Ceg1p. Here we localize the
guanylyltransferase-binding and guanylyltransferase-stimulation functions
of Cet1p to a 21-amino acid segment from residues 239 to 259. The
guanylyltransferase-binding domain is located on the protein surface, as
gauged by protease sensitivity, and is conserved in the Candida albicans
RNA triphosphatase CaCet1p. Alanine-cluster mutations of a WAQKW motif
within this segment abolish guanylyltransferase- binding in vitro and Cet1p
function in vivo, but do not affect the triphosphatase activity of Cet1p.
Proteolytic footprinting experiments provide physical evidence that Cet1p
interacts with the C-terminal domain of Ceg1p. Trypsin-sensitive sites of
Ceg1p that are shielded from proteolysis when Ceg1p is bound to Cet1p are
located between nucleotidyl transferase motifs V and VI.
ARTICLES
An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
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