Nucleic Acids Research, Vol 26, Issue 14 3410-3417, Copyright © 1998 by Oxford University Press
SR Soltaninassab, JG McAfee, L Shahied-Milam and WM LeStourgeon
Through the use of various non-equilibrium RNA binding techniques, the C
protein tetramer of mammalian40S hnRNP particles has been characterized
previously as a poly(U) binding protein with specificity for the
pyrimidine-rich sequences that often precede 3' intron-exon junctions. C
protein has also been characterized as a sequence- independent RNA
chaperonin that is distributed along nascent transcripts through
cooperative binding and as a protein ruler that defines the length of RNA
packaged in 40S monoparticles. In this study fluorescence spectroscopy was
used to monitor C protein-oligonucleotide binding in a competition binding
assay under equilibrium conditions. Twenty nucleotide substrates
corresponding to polypyrimidine tracts from IVS1 of the adenovirus-2 major
late transcript, the adenovirus-2 oncoprotein E1A 3' splice site, IVS2 of
human alpha-tropomyosin, the consensus polypyrimidine tract for U2AF65,
AUUUA repeats and r(U)20were used as competitors. A 20 nt beta-globin
intronic sequence and a randomly generated oligo were used as competitor
controls. These studies reveal that native C protein possesses no enhanced
affinity for uridine-rich oligonucleotides, but they confirm the enhanced
affinity of C protein for an oligonucleotide identified as a high affinity
substrate through selection and amplification. Evidence that the affinity
of C protein for the winner sequence is due primarily to its unique
structure or to a unique context is seen in its retained substrate affinity
when contiguous uridines are replaced with contiguous guanosines.
ARTICLES
Oligonucleotide binding specificities of the hnRNP C protein tetramer
Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235, USA.
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