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

AUTOR(ES)

Hemmerich, P

RESUMO

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.

Documentos Relacionados

• Identification of a Candida utilis gene encoding ribosomal protein L7: evidence for two divergent subclasses of the eukaryotic ribosomal protein L7 family.
• Archaeal ribosomal protein L7 is a functional homolog of the eukaryotic 15.5kD/Snu13p snoRNP core protein
• The Requirement for Ribosomal Proteins L7 and L12 in Peptide-Chain Termination
• A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis
• The Identification of the Eukaryotic Ribosomal Proteins Homologous with Escherichia coli Proteins L7 and L12