Human RNA-binding protein

#This invention relates to nucleic acid and amino acid sequences of a novel human RNA-binding protein and to the use of these sequences in the diagnosis, prevention, and treatment of cancer and inflammatory diseases.

#The regulation of gene expression and cellular function is controlled at many different levels in eukaryotic cells. Evidence has been accumulated over the past few years pointing to the importance of mRNA stability, localization, and translation in these processes during development (Berleth, T. et al. (1988) EMBO J. 7:1749-1756; St. Johnston, D. et al. (1991) Cell 92:171-178); Ferrandon, D. et al. (1994) Cell 79:1221-1232) and maintenance of the differentiated phenotype (Wilhelm, J. E. et al. (1993) J. Cell Biol. 123:269-274; Klausner, R. D. et al. (1993) Cell 72:1-28; Hentze, M. W. (1995) Curr. Op. Biol. 7:393-398).

#Central to the regulation of these processes are proteins which recognize and bind to specific primary sequences or secondary structures in nucleic acids. Increasing numbers of these proteins are being identified, and a variety of nucleic acid-binding motifs have been recognized (reviewed by Burd, G. C. and G. Dreyfuss (1994) Science 265:615-621). The Y-box family of proteins is perhaps the most evolutionarily conserved group of nucleic acid-binding proteins known. The binding domain of the 70-residue E. coli CS7.4 cold-shock protein is 43% identical to the binding domain of vertebrate Y-box family members. Diverse molecular functions are ascribed to eukaryotic members of the Y-box family including transcription factors and translation control proteins (for reviews, see: Wolffe, A. P. (1994) Bioessays 16:245-251; Burd, C. G. and G. Dreyfuss, supra).

#FIG. 1 shows the amino acid sequence (SEQ ID NO: 1) and nucleic acid sequence (SEQ ID NO:2) of HRNABP. The alignment was produced using "MACDNASIS PRO" software (Hitachi Software Engineering Co., Ltd., San Bruno, Calif.).

#FIG. 2 shows the amino acid sequence alignment between HRNABP (SEQ ID NO:1) and rat brain RNA-binding protein PIPPin (G1050754; SEQ ID NO:3). The alignment was produced using the multisequence alignment program of DNASTAR software (DNASTAR Inc, Madison Wis.).

#FIG. 3 shows the hydrophobicity plot (MACDNASIS PRO software) for HRNABP, SEQ ID NO:1. Positive X axis reflects amino acid position, and the negative Y axis reflects hydrophobicity.

#Before the present proteins, nucleotide sequences, and methods are described, it is understood that this invention is not limited to the particular methodology, protocols, cell lines, vectors, and reagents described as these may vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention which will be limited only by the appended claims.

#It must be noted that as used herein and in the appended claims, the singular forms "a", "an", and "the" include plural reference unless the context clearly dictates otherwise. Thus, for example, reference to "a host cell" includes a plurality of such host cells, reference to the "antibody" is a reference to one or more antibodies and equivalents thereof known to those skilled in the art, and so forth.

#Unless defined otherwise, all technical and scientific terms used herein have the same meanings as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, the preferred methods, devices, and materials are now described. All publications mentioned herein are incorporated herein by reference for the purpose of describing and disclosing the cell lines, vectors, and methodologies which are reported in the publications which might be used in connection with the invention. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.