Zinc finger-like motifs in rat ribosomal proteins S27 and S29.

AUTOR(ES)

Chan, Y L

RESUMO

The primary structures of the rat 40S ribosomal subunit proteins S27 and S29 were deduced from the sequences of nucleotides in recombinant cDNAs and confirmed by determination of amino acid sequences in the proteins. Ribosomal protein S27 has 83 amino acids and the molecular weight is 9,339. Hybridization of cDNA to digests of nuclear DNA suggests that there are 4-6 copies of the S27 gene; the mRNA for the protein is about 620 nucleotides in length. Ribosomal protein S29 has 55 amino acids and the molecular weight is 6,541. There are 14-17 copies of the S29 gene and its mRNA is about 500 nucleotides in length. Rat ribosomal protein S29 is related to several members of the archaebacterial and eubacterial S14 family of ribosomal proteins. S27 and S29 have zinc finger-like motifs as do other proteins from eukaryotic, archaebacterial, eubacterial, and mitochondrial ribosomes. Moreover, ribosomes and ribosomal subunits appear to contain zinc and iron as well.

Documentos Relacionados

• An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif.
• Finger-like lysing patterns of blood clots.
• Fluorescent-Antibody Study of Natural Finger-Like Zooloeae
• The two zinc finger-like domains of GATA-1 have different DNA binding specificities.
• A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.