Nucleic Acids Research, Vol 24, Issue 15 2990-2997, Copyright © 1996 by Oxford University Press
A Inoue, KP Takahashi, M Kimura, T Watanabe and S Morisawa
S1 proteins A-D constitute a nuclear protein family that are liberated
rapidly in a set from chromatin by mild digestion with a DNA or RNA
hydrolyzing enzyme. With an anti-S1-protein B antiserum that reacted with
B2, C1 and D1, a cDNA clone, pS1-1, was obtained, which encoded a protein
of 852 amino acids. The S1-1 protein, encoded within the cells by a mRNA of
3480 nt, was a novel protein and could be distinguished from the S1
proteins B, C and D by their amino acid sequences. The S-1- 1 protein
synthesized by in vitro translation bound to RNA homopolymers, with a
preference for G and U polyribonucleotides and little for poly(A). The
protein contained two tandem RNP motifs and several intriguing sequences,
such as a novel repeat of five octamers with a consensus sequence
DP-S(Q/G)YYY and a potentially perfect amphipathic alpha-helix of five
turns with basic and acidic amino acids positioned in an ordered way. The
two RNP motif sequences were similar, although homologies were low, to the
RNP motif sequences of yeast NSR1 protein, animal nucleolins, Drosophila
hnRNP Al and tobacco chloroplast RNP precursor protein, suggesting a
functional uniqueness of the S1-1 protein in RNA metabolism and also the
evolution of its RNP motif structure before plants and animals diverged.
These results indicate that the S1-1 protein encoded by the cDNA is a new
class of RNA binding protein.
ARTICLES
Molecular cloning of a RNA binding protein, S1-1
Department of Biochemistry, Osaka City University Medical School, Japan.
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