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By subtractive screening of a library made from mRNA of lipopolysaccharide (LPS)-stimulated mouse B lymphocytes we isolated cDNA-clones encoding the ribosomal protein L7. Human L7 mRNA was cloned from activated T-lymphocytes. Although no specific function of L7 in the translation apparatus is known as yet, it should be a critical one as indicated by its high degree of structural conservation during evolution and its regulated expression in lymphoid cells. Human and rodent L7 proteins carry sequences similar to the basic-region-leucine-zipper(BZIP)-motif of DNA-binding eucaryotic transcription factors. We show here that the region of L7 carrying the latter motif mediates L7-dimerization and stable binding to DNA and RNA. A preferential binding to RNA-structures is demonstrated.

Structural and functional properties of ribosomal protein L7 from humans and rodents