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(Received for publication, January 7, 1997, and in revised form, February 12, 1997)
From the Department of Molecular Biology and Microbiology, Tufts
University School of Medicine, Boston, Massachusetts 02111-1800
Cleavage of pre-mRNA during 3
Volume 272, Number 16,
Issue of April 18, 1997
pp. 10831-10838
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
-end formation
in yeast requires two protein factors, cleavage factor I (CF I) and
cleavage factor (CF II). A 5300-fold purification of CF II indicates
that four polypeptides of 150, 105, 100, and 90 kDa copurify with CF II
activity. The 150-kDa protein is recognized by antibodies against Cft1,
the yeast homologue of the 160-kDa subunit of the mammalian cleavage/polyadenylation specificity factor (CPSF). The 100-kDa subunit
is identical to Brr5/Ysh1, a yeast protein with striking similarity to
the 73-kDa subunit of CPSF. The 105-kDa protein, designated Cft2
(cleavage factor two) exhibits significant homology to the CPSF 100-kDa
subunit. Cft2 is cross-linked to pre-mRNA substrate containing the
poly(A) site and wild type upstream and downstream flanking sequences,
but not to precleaved RNA lacking downstream sequences or to substrate
in which the (UA)6 processing signal has been
deleted. The specific binding of Cft2 to the RNA substrate is
ATP-dependent, in agreement with the requirement of ATP for
cleavage. The sequence-specific binding of Cft2 and the similarities of
CF II subunits to those of CPSF supports the hypothesis that CF II
functions in the cleavage of yeast mRNA 3-ends in a manner
analagous to that of CPSF in the mammalian system. These results
provide additional evidence that certain features of the molecular
mechanism of mRNA 3-end formation are conserved between yeast and
mammals, but also highlight unexpected differences.
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