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Nucleic Acids Research, 1987, Vol. 15, No. 3 987-1003
© 1987


Articles

Structural analysis of the Drosophila rpA1 gene, a member of the eucaryotic ‘A’ type ribosomal protein family

Su Qian, Jing-Yu Zhang1, Mark A. Kay and Marcelo Jacobs-Lorena*

Department of Developmental Genetics and Anatomy, School of Medicine, Case Western Reserve University 2119 Abington Road, Cleveland, OH 44106, USA

*To whom correspondence should be addressed

Received October 7, 1986. Revised January 9, 1987. Accepted January 9, 1987.

The expression of ribosomal protein (r-protein) genes is uniquely regulated at the translational level during early development of Drosophila. Here we report results of a detailed analysis of the r-protein rpAl gene. A cloned DNA sequence coding for rpAl has been identified by hybrid-selected translation and amino acid composition analysis. The rpAl gene was localized to polytene chromosome band 53CD. The nucleotide sequence of the rpAl gene and its cDNA have been determined. rpAl is a single copy gene and sequence comparison between the gene and its cDNA indicates that this r-protein gene is intronless. Allelic restriction site polymorphisms outsite of the gene were observed, while the coding sequence is well conserved between two Drosophila strains. The protein has unusual domains rich in Ala and charged residues. The rpAl is homologous to the "A" family of eucaryotic acidic r-proteins which are known to play a key role in the initiation and elongation steps of protein synthesis.


1Present address: Department of Biochemistry, Tianjing Medical College, Tianjing, People's Republic of China


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