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Originally published In Press as doi:10.1074/jbc.M910448199 on March 22, 2000

J. Biol. Chem., Vol. 275, Issue 23, 17241-17248, June 9, 2000
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Functional Characterization of Yeast Mitochondrial Release Factor 1*

Marjan E. Askarian-Amiri, Herman J. PelDagger , Diane Guévremont, Kim K. McCaughan, Elizabeth S. Poole, Vicki G. Sumpter, and Warren P. Tate§

From the Department of Biochemistry and Centre for Gene Research, University of Otago, P. O. Box 56, 9015 Dunedin, New Zealand

The yeast Saccharomyces cerevisiae mitochondrial release factor was expressed from the cloned MRF1 gene, purified from inclusion bodies, and refolded to give functional activity. The gene encoded a factor with release activity that recognized cognate stop codons in a termination assay with mitochondrial ribosomes and in an assay with Escherichia coli ribosomes. The noncognate stop codon, UGA, encoding tryptophan in mitochondria, was recognized weakly in the heterologous assay. The mitochondrial release factor 1 protein bound to bacterial ribosomes and formed a cross-link with the stop codon within a mRNA bound in a termination complex. The affinity was strongly dependent on the identity of stop signal. Two alleles of MRF1 that contained point mutations in a release factor 1 specific region of the primary structure and that in vivo compensated for mutations in the decoding site rRNA of mitochondrial ribosomes were cloned, and the expressed proteins were purified and refolded. The variant proteins showed impaired binding to the ribosome compared with mitochondrial release factor 1. This structural region in release factors is likely to be involved in codon-dependent specific ribosomal interactions.

* This work was supported by the Royal Society of New Zealand Marsden Fund and by the Human Frontier Science Program Grant RG32/97.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: DSM Food Specialties, DSM Gist 426-0295, P. O. Box 1, 2600 MA Delft, Netherlands.

§ To whom correspondence should be addressed. Tel.: 64-3-479-7841; Fax: 64-3-479-7866; E-mail: warren.tate@stonebow.otago.ac.nz.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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