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J. Biol. Chem., Vol. 277, Issue 22, 19639-19648, May 31, 2002
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From the Molecular Biology Program, Sloan-Kettering Institute,
New York, New York 10021
Elongating RNA polymerase II is targeted by
macromolecular assemblies that regulate mRNA synthesis and
processing. The capping apparatus is the first of the assemblies to act
on the nascent pre-mRNA. Although recruitment of the capping
enzymes to the transcription complex is dependent on phosphorylation of
the C-terminal domain of the Rpb1 subunit of polymerase II
(Pol-II), there may be additional levels of control that coordinate
capping with elongation. Here we show that the triphosphatase (Pct1)
and guanylyltransferase (Pce1) enzymes of the fission yeast capping
apparatus bind independently to the elongation factor Spt5. The
C-terminal domain of the 990-amino acid Schizosaccharomyces
pombe Spt5 protein, composed of repeats of a nonapeptide
motif (consensus sequence TPAWNSGSK), is necessary and sufficient for
binding to the capping enzymes in vivo (in a two-hybrid
assay) and in vitro. As few as four nonamer repeats suffice
for Spt5 binding to Pct1 in vitro, whereas six repeats are
required for Spt5 binding to Pce1. A 116-amino acid fragment of the
guanylyltransferase Pce1 suffices for binding to the Spt5 C-terminal
domain (CTD) but not for binding to the Pol-II CTD. Pct1 and Pce1 can
bind simultaneously to the Spt5 CTD in vitro. We find that
Spt5 is essential for viability of S. pombe and that it
interacts in vivo with S. pombe Spt4 via a
central domain distinct from the Spt5 CTD. We suggest that Spt5-induced
arrest of elongation at promoter proximal positions ensures a temporal
window for recruitment of the capping enzymes.
To whom correspondence should be addressed. E-mail:
s-shuman@ ski.mskcc.org.
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