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Mol Cell Biol. 1992 April; 12(4): 1680-1686

Fine-structure map of the human ribosomal protein gene RPS14.

Division of Biology, Kansas State University, Manhattan 66506.

ABSTRACT

We have used polymerase chain reaction-mediated chemical mutagenesis (J.-J. Diaz, D. D. Rhoads, and D. J. Roufa, BioTechniques 11:204-211, 1991) to analyze the genetic fine structure of a human ribosomal protein gene, RPS14. Eighty-three DNA clones containing 158 random single-base substitution mutations were isolated. Mutant RPS14 alleles were tested for biological activity by transfection into cultured Chinese hamster cells. The resulting data permitted us to construct a map of the S14-coding sequence that is comparable to available fine-structure genetic maps of many prokaryotic and lower eukaryotic gene loci. As predicted from the multiplicity of protein-protein and protein-RNA interactions required for ribosomal protein transport and assembly into functional ribosomal subunits, the distribution of null mutations indicated that S14 is composed of multiple, functionally distinct polypeptide domains. Two of the protein's internal domains, designated domains B and D, were essential for S14 biological activity. In contrast, mutations which altered or deleted S14's amino-terminal 20 amino acid residues (domain A) had no observable effect on the protein's assembly and function in mammalian ribosomes. Interestingly, S14 structural domains deduced by in vitro mutagenesis correlate well with the RPS14 gene's exon boundaries.

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• Martin-Nieto, J, Roufa, D. (1997). Functional analysis of human RPS14 null alleles. J. Cell Sci. 110: 955-963 [Abstract]  
• Tasheva, E S, Roufa, D J (1995). Regulation of human RPS14 transcription by intronic antisense RNAs and ribosomal protein S14.. Genes Dev. 9: 304-316 [Abstract]