Nucleic Acids Research, Vol 24, Issue 16 3222-3228, Copyright © 1996 by Oxford University Press
E Chu, T Cogliati, SM Copur, A Borre, DM Voeller, CJ Allegra and S Segal
We developed an immunoprecipitation-RNA-random PCR (rPCR) method to isolate
cellular RNA sequences that bind to the folate-dependent enzyme thymidylate
synthase (TS). Using this approach, nine different cellular RNAs that
formed a ribonucleoprotein (RNP) complex with thymidylate synthase (TS) in
human colon cancer cells were identified. RNA binding experiments revealed
that seven of these RNAs bound TS with relatively high affinity (IC50
values ranging from 1.5 to 6 nM). One of the RNAs was shown to encode the
interferon (IFN)-induced 15 kDa protein. Western immunoblot analyses
demonstrated that the level of IFN-induced 15 kDa protein was significantly
decreased in human colon cancer H630- R10 cells compared with parent H630
cells. While the level of IFN- induced 15 kDa mRNA expression was the same
in parent and TS- overexpressing cell lines, the level of IFN-induced 15
kDa RNA bound to TS in the form of a RNP complex was markedly higher in
H630-R10 cells relative to parent H630 cells. These studies begin to define
a number of cellular target RNA sequences with which TS interacts and
suggest that these TS protein-cellular RNA interactions may have a
biological role.
ARTICLES
Identification of in vivo target RNA sequences bound by thymidylate synthase
NCI-Navy Medical Oncology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20889-5105, USA.
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