Nucleic Acids Research, Vol 26, Issue 15 3460-3467, Copyright © 1998 by Oxford University Press
SA Wilson, EC Brown, AJ Kingsman and SM Kingsman
A northwestern screen of a CHO-K1 cell line cDNA library with radiolabelled
HIV-1 TAR RNA identified a novel TAR RNA interacting protein, TRIP. The
human trip cDNA was also cloned and its expression is induced by phorbol
esters. The N-terminus of TRIP shows high homology to the coiled coil
domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of
Flightless I (FLI) and the interaction of TRIP with the FLI LRR has been
confirmed in vitro . TRIP does not bind single stranded DNA or RNA
significantly and binds double stranded DNA weakly. In contrast, TRIP binds
double stranded RNA with high affinity and two molecules of TRIP bind the
TAR stem. The RNA binding domain has been identified and encompasses a
lysine-rich motif. A TRIP-GFP fusion is localised in the cytoplasm and
excluded from the nucleus. FLI has a C-terminal gelsolin-like domain which
binds actin and therefore the association of TRIP with the FLI LRR may
provide a link between the actin cytoskeleton and RNA in mammalian cells.
ARTICLES
TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
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