Molecular characterization of the transcription termination factor from human mitochondria

A. Daga, V. Micol, D. Hess, R. Aebersold, G. Attardi

Research output: Contribution to journalArticlepeer-review


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 ~34-kDa molecular mass and one of ~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.

Original languageEnglish
Pages (from-to)8123-8130
Number of pages8
JournalJournal of Biological Chemistry
Issue number11
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Molecular characterization of the transcription termination factor from human mitochondria'. Together they form a unique fingerprint.

Cite this