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Nucleic Acids Research, 1992, Vol. 20, No. 17 4423-4428
© 1992

MOLECULAR BIOLOGY

Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure

Herman J. Pel, Martijn Rep and Leslie A. Grivell*

Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam Kruislaan 318, 1098 SM Amsterdam, The Netherlands

*To whom correspondence should be addressed

Received June 25, 1992. Revised August 13, 1992. Accepted August 13, 1992.

We have recently reported the cloning and sequencing of the gene for the mitochondrial release factor mRF-1. mRF-1 displays high sequence similarity to the bacterial release factors RF-1 and RF-2. A database search for proteins resembling these three factors revealed high similarities to two amino acid sequences deduced from unassigned genomic reading frames in Escherichia coli and Bacillus subtilis. The amino acid sequence derived from the Bacillus reading frame is 47% identical to E.coli and Saimonella typhimurium RF-2, strongly suggesting that it represents B.subtills RF-2. Our comparison suggests that the expression of the B.subtilis gene is, like that of the E.coli and S. typhimurium RF-2 genes, autoregulated by a stop codon dependent +1 frameshift. A comparison of prokaryotic and mitochondrial release factor sequences, including the putative B.subtilis RF-2, leads us to propose a five-domain model for release factor structure. Possible functions of the various domains are discussed.


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