Cell-free translation of mitochondrial nicotinamide nucleotide transhydrogenase

Author:

Carlenor Elisabeth1,Joste Vigg1,Nelson B. Dean1,Rydström Jan1

Affiliation:

1. Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden

Abstract

Mammalian nicotinamide nucleotide transhydrogenase is translated as a 5000 daltons larger molecular weight precursor in a cell-free system programmed with rat liver polysomes. The mature rat liver enzyme had the same molecular weight as the purified beef heart enzyme, 115 000 daltons. The precursor was not processed in vitro by liver mitochondria or by a rat liver mitochondrial matrix fraction, nor did it appear to bind to mitochondria. In contrast, pre-FeS protein of the cytochrome bc1 complex was processed in the same samples by both mitochondria and matrix, suggesting an important difference in the processing mechanisms or in the efficiency of processing of the two precursors.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference25 articles.

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2. Fisher RR & Earle SR (1982) In: The Pyridine Nucleotide Coenzymes (Everse J, Andersson B & You K, eds), pp 280?324, Academic Press, New York.

3. Rydström J, Persson B & Carlenor E (1985) In: Coenzymes and Cofactors (Dolphin D, Poulson R & Avramovic O, eds), Wiley and Sons, New York, in press.

4. Schatz G (1983) Cell32, 316?318.

5. Hay R, Böhni P & Gasser S (1984) Biochim. Biophys. Acta779, 65?87.

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