Nucleic Acids Research, Vol 27, Issue 8 1926-1934, Copyright © 1999 by Oxford University Press
G Triqueneaux, M Velten, P Franzon, F Dautry and H Jacquemin-Sablon
The human unr gene encodes an 85 kDa protein which contains five cold shock
domains (CSD). The capacity of Unr to interact in vitro with RNA and its
intracellular localization suggest that Unr could be involved in some
aspect of cytoplasmic mRNA metabolism. As a step towards identification of
Unr mRNA targets, we investigated the RNA-binding specificity of Unr by an
in vitro selection approach (SELEX). Purine- rich sequences were selected
by Unr, leading to the identification of two related consensus sequences
characterized by a conserved core motif AAGUA/G or AACG downstream of a
purine stretch. These consensus sequences are 11-14 nt long and appear
unstructured. RNAs containing a consensus sequence were bound specifically
by Unr with an apparent dissociation constant of 1 x 10(-8) M and both
elements, the 5' purine stretch and the core motif, were shown to
contribute to the high affinity. When the N-terminal and C-terminal CSD
were analyzed individually, they exhibited a lower affinity than Unr for
winner sequences (5- and 100-fold, respectively) but with similar binding
specificity. Two combinations of CSDs, CSD1-2-3 and CSD1*2-3-4-5 were
sufficient to achieve the high affinity of Unr, indicating some redundancy
between the CSDs of Unr for RNA recognition. The SELEX- generated consensus
motifs for Unr differ from the AACAUC motif selected by the Xenopus Y-box
factor FRGY2, indicating that a diversity of RNA sequences could be
recognized by CSD-containing proteins.
ARTICLES
RNA binding specificity of Unr, a protein with five cold shock domains
CNRS UPR 9044, Genetique Moleculaire et Integration des Fonctions Cellulaires, Institut de Recherches sur le Cancer, BP 8, 94801 Villejuif, France.
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