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Nucleic Acids Research, 1993, Vol. 21, No. 3 649-655
© 1993

MOLECULAR BIOLOGY

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

Yuen-Ling Chan, Katsuyuki Suzuki, Joe Olvera and Ira G. Wool*

Department of Biochemistry and Molecular Biology, The University of Chicago Chicago, IL 60637, USA

*To whom correspondence should be addressed

Received September 24, 1992. Revised December 12, 1992. Accepted December 12, 1992.

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 nucieotldes 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, archaebacteriai, eubacterial, and mltochondrial ribosomes. Moreover, ribosomes and ribosomal subunits appear to contain zinc and iron as well.


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