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Nucleic Acids Research, 1991, Vol. 19, No. 6 1273-1278
© 1991


MOLECULAR BIOLOGY

A differentially expressed murine RNA encoding a protein with similarities to two types of nucleic acid binding motifs

M. Ayane, U. Preuss, G. Köhler and P.J. Nielsen*

Max Planck Institut für Immunbiologie Stübeweg 51,D-7800 Freiburg i.Br., FRG

* To whom correspondence should be addressed

Received December 11, 1990. Revised February 15, 1991. Accepted February 15, 1991.

Using differential screening, a muiine cDNA, termed X16, was isolated corresponding to an mRNA which is more strongly expressed in pre-B cell lines relative to mature B-cell lines. The complete coding sequence of the mRNA predicts a l9kD protein with two domains connected by a proline-rich spacer. The N-terminal domain of about 90 amino acids encodes an RNA binding motif including the ribonucleoprotein consensus octapeptide found in one class of RNA binding proteins and highly conserved from yeast to man. Within the very basic C-terminal domain of about 60 amino acids, several copies of two different peptides are found which are also present in several proteins which bind DNA or RNA. The expression of X16 Is not limited to the lymphold lineage. In adult mice, although the strongest expression was seen in thymus, mRNA was also found In testis, brain, spleen, and very low in heart. X16 mRNA was not detected in liver and kidney. In tissue culture, the expression of X16 mRNA can be induced by serum. The conserved protein motifs and expression pattern suggest that X16 could be involved in RNA processing correlating with cellular proliferation.


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