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Published April 1, 1977 | public
Journal Article Open

Association of a protein structure of probable membrane derivation with HeLa cell mitochondrial DNA near its origin of replication

Abstract

Almost all (about 95%) of the mitochondrial DNA molecules released by Triton X-100 lysis of HeLa cell mitochondria in the presence of 0.15 M salt are associated with a single protein-containing structure varying in appearance between a 10-20 nm knob and a 100-500 nm membrane-like patch. Analysis by high resolution electron microscopy and by polyacrylamide gel electrophoresis after cleavage of mitochondrial DNA with the endonucleases EcoRI, HindIII, and Hpa II has shown that the protein structure is attached to the DNA in the region of the D-loop, and probably near the origin of mitochondrial DNA replication. The data strongly suggest that HeLa cell mitochondrial DNA is attached in vivo to the inner mitochondrial membrane at or near the origin of replication, and that a membrane fragment of variable size remains associated with the DNA during the isolation. After sodium dodecyl sulfate extraction of mitochondrial DNA, a small 5-10 nm protein is found at the same site on a fraction of the mitochondrial DNA molecules.

Additional Information

© 1977 by the National Academy of Sciences. Communicated by Norman Davidson, November 29, 1976. We wish to thank Ms. D. Ojala and Dr. A. Szalay for advice in the polyacrylamide gel electrophoretic analysis. The help of Ms. A. Drew and Ms. G. Engel is gratefully acknowledged. This work has been supported by a research grant from the U.S. Public Health Service (GM-11726) and a fellowship of the Deutsche Forschungsgemeinschaft to M.A.

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August 22, 2023
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