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Journal of Bacteriology, May 1999, p. 2930-2937, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Ribosomal -1 Frameshifting during Decoding of Bacillus subtilis cdd Occurs at the Sequence CGA AAG

Nina Mejlhede,1 John F. Atkins,2 and Jan Neuhard1,*

Center for Enzyme Research, Institute of Molecular Biology, University of Copenhagen, DK-1307 Copenhagen K, Denmark,1 and Department of Human Genetics, University of Utah, Salt Lake City, Utah 84112-533022

Received 16 November 1998/Accepted 11 February 1999

During translation of the Bacillus subtilis cdd gene, encoding cytidine deaminase (CDA), a ribosomal -1 frameshift occurs near the stop codon, resulting in a CDA subunit extended by 13 amino acids. The frequency of the frameshift is approximately 16%, and it occurs both when the cdd gene is expressed from a multicopy plasmid in Escherichia coli and when it is expressed from the chromosomal copy in B. subtilis. As a result, heterotetrameric forms of the enzyme are formed in vivo along with the dominant homotetrameric species. The different forms have approximately the same specific activity. The cdd gene was cloned in pUC19 such that the lacZ' gene of the vector followed the cdd gene in the -1 reading frame immediately after the cdd stop codon. By using site-directed mutagenesis of the cdd-lacZ' fusion, it was shown that frameshifting occurred at the sequence CGA AAG, 9 bp upstream of the in-frame cdd stop codon, and that it was stimulated by a Shine-Dalgarno-like sequence located 14 bp upstream of the shift site. The possible function of this frameshift in gene expression is discussed.

* Corresponding author. Mailing address: Department of Biological Chemistry, Sølvgade 83, DK-1307 Copenhagen K, Denmark. Phone: (45) 35 32 20 02. Fax: (45) 35 32 20 40. E-mail: neuhard{at}mermaid.molbio.ku.dk.

Journal of Bacteriology, May 1999, p. 2930-2937, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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