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Molecular characterization of the transcription termination factor from human mitochondria

Daga, Andrea and Micol, Vicente and Hess, Daniel and Aebersold, Ruedi and Attardi, Giuseppe (1993) Molecular characterization of the transcription termination factor from human mitochondria. Journal of Biological Chemistry, 268 (11). pp. 8123-8130. ISSN 0021-9258.

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The transcription termination factor (mTERF), which plays a central role in the control of mitochondrial rRNA and mRNA synthesis in mammalian mitochondria, has been previously identified and purified by DNA affinity chromatography from a human mitochondrial lysate (Kruse, B., Narasimhan, N., and Attardi, G. (1989) Cell 58, 391-397). In the present work, this factor has been characterized as to its protein composition and the activities of the protein components. Three polypeptides, two of approximately 34-kDa molecular mass and one of approximately 31 kDa, were shown to be associated with the specific DNA binding and footprinting activity of the factor, with the 31-kDa component having a much lower affinity for the recognition sequence than the 34-kDa components. On the other hand, the transcription termination activity, as assayed in an in vitro system, was found to be associated exclusively with the two 34-kDa polypeptides. Mass spectroscopic analysis of tryptic peptides derived from highly purified polypeptides indicated that all three polypeptides share regions with common sequences. The evidence obtained suggests that differential phosphorylation is not responsible for the difference in electrophoretic mobility of the three polypeptides.

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Additional Information:Copyright © 1993 by the American Society for Biochemistry and Molecular Biology. (Received for publication, September 10, 1992) The expert technical assistance of Arger Drew, Lisa Tefo, and Hamish Morrison is gratefully acknowledged, and we thank Dr. Patricio Fernández-Silva for help in the preparation of the mTERF protein and Dr. Tom Covey for technical advice. These investigations were supported by National Institutes of Health Grant GM-11726 (to G.A.) and grants from the Department of Industry, Science, and Technology of Canada and the Medical Research Council of Canada (to R.A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. [V.M. was the] [r]ecipient of a scholarship from the Fulbright/Spanish Ministry of Education and Science Visiting Scholar Program. [R.A. was the] [r]ecipient of a scholarship from the Medical Research Council of Canada.
Issue or Number:11
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ID Code:6980
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Deposited On:04 Jan 2007
Last Modified:02 Oct 2019 23:37

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