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Vol. 13, No. 4, pp. 437-448, February 15, 1999
1 Department of Biochemistry, University of Cambridge, Old
Addenbrooke's Site, Cambridge, CB2 1GA, UK; 2 Ludwig
Institute for Cancer Research, Middlesex Hospital, University College
Branch, London, W1P 8BT, UK
Initiation of translation of the animal picornavirus RNAs occurs via
a mechanism of direct ribosome entry, which requires a segment of the
5' UTR of the RNA, known as the internal ribosome entry site
(IRES). In addition, translation of the enterovirus and rhinovirus
(HRV) subgroups requires cellular trans-acting factors that are
absent from, or limiting in rabbit reticulocytes, but are more abundant
in HeLa cell extracts. It has been shown previously that HeLa cells
contain two separable activities, each of which independently
stimulates HRV IRES-dependent translation when used to supplement
reticulocyte lysate; one of these activities was identified as
polypyrimidine tract-binding protein (PTB). Here, the purification of
the second activity is achieved by use of an RNA-affinity column based
on the HRV 5' UTR. It comprises two components: a 38-kD protein
(p38), which is a novel member of the GH-WD repeat protein family and
has no intrinsic RNA-binding activity; and a 96- to 97-kD protein
doublet, which was identified as unr, an RNA-binding protein with five
cold-shock domains. Coimmunoprecipitation with antibodies against
either protein shows that the two proteins interact with each other,
and thus p38 is named unrip (unr-interacting protein). Recombinant unr acts synergistically with
recombinant PTB to stimulate translation dependent on the rhinovirus
IRES. In contrast, unr did not significantly augment the PTB-dependent stimulation of poliovirus IRES activity.
[Key Words: Human rhinovirus; poliovirus; translation initiation; IRES; RNA-binding proteins]
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