Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Finnzymes

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 6 August 1993:
Vol. 261. no. 5122, pp. 765 - 769
DOI: 10.1126/science.7688144

Articles

Science, Vol 261, Issue 5122, 765-769
Copyright © 1993 by American Association for the Advancement of Science


articles

Primers for mitochondrial DNA replication generated by endonuclease G

J Cote and A Ruiz-Carrillo

Cancer Research Center, Medical School of Laval University, L'Hotel-Dieu de Quebec, Canada.

Endonuclease G (Endo G) is widely distributed among animals and cleaves DNA at double-stranded (dG)n.(dC)n and at single-stranded (dC)n tracts. Endo G is synthesized as a propeptide with an amino-terminal presequence that targets the nuclease to mitochondria. Endo G can also be detected in extranucleolar chromatin. In addition to deoxyribonuclease activities, Endo G also has ribonuclease (RNase) and RNase H activities and specifically cleaves mouse mitochondrial RNA and DNA-RNA substrates containing the origin of heavy-strand DNA replication (OH). The cleavage sites match those found in vivo, indicating that Endo G is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
EXOG, a novel paralog of Endonuclease G in higher eukaryotes.
I. A. Cymerman, I. Chung, B. M. Beckmann, J. M. Bujnicki, and G. Meiss (2008)
Nucleic Acids Res. 36, 1369-1379
   Abstract »    Full Text »    PDF »
Expression of a novel non-coding mitochondrial RNA in human proliferating cells.
J. Villegas, V. Burzio, C. Villota, E. Landerer, R. Martinez, M. Santander, R. Martinez, R. Pinto, M. I. Vera, E. Boccardo, et al. (2007)
Nucleic Acids Res. 35, 7336-7347
   Abstract »    Full Text »    PDF »
Nuclear translocation of EndoG at the initiation of disuse muscle atrophy and apoptosis is specific to myonuclei.
E. E. Dupont-Versteegden, B. A. Strotman, C. M. Gurley, D. Gaddy, M. Knox, J. D. Fluckey, and C. A. Peterson (2006)
Am J Physiol Regulatory Integrative Comp Physiol 291, R1730-R1740
   Abstract »    Full Text »    PDF »
Mitochondrial Functions and Estrogen Receptor-dependent Nuclear Translocation of Pleiotropic Human Prohibitin 2.
K. Kasashima, E. Ohta, Y. Kagawa, and H. Endo (2006)
J. Biol. Chem. 281, 36401-36410
   Abstract »    Full Text »    PDF »
Endonuclease G: A role for the enzyme in recombination and cellular proliferation.
K.-J. Huang, C.-C. Ku, and I. R. Lehman (2006)
PNAS 103, 8995-9000
   Abstract »    Full Text »    PDF »
Mature DIABLO/Smac Is Produced by the IMP Protease Complex on the Mitochondrial Inner Membrane.
L. Burri, Y. Strahm, C. J. Hawkins, I. E. Gentle, M. A. Puryer, A. Verhagen, B. Callus, D. Vaux, and T. Lithgow (2005)
Mol. Biol. Cell 16, 2926-2933
   Abstract »    Full Text »    PDF »
Generation and Characterization of Endonuclease G Null Mice.
R. A. Irvine, N. Adachi, D. K. Shibata, G. D. Cassell, K. Yu, Z. E. Karanjawala, C.-L. Hsieh, and M. R. Lieber (2005)
Mol. Cell. Biol. 25, 294-302
   Abstract »    Full Text »    PDF »
Vulnerability of Central Neurons to Secondary Insults after In Vitro Mechanical Stretch.
M. Arundine, M. Aarts, A. Lau, and M. Tymianski (2004)
J. Neurosci. 24, 8106-8123
   Abstract »    Full Text »    PDF »
Endonuclease G is required for early embryogenesis and normal apoptosis in mice.
J. Zhang, M. Dong, L. Li, Y. Fan, P. Pathre, J. Dong, D. Lou, J. M. Wells, D. Olivares-Villagomez, L. Van Kaer, et al. (2003)
PNAS 100, 15782-15787
   Abstract »    Full Text »    PDF »
A Ca2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within the mitochondrial matrix.
A. M. Davies, S. Hershman, G. J. Stabley, J. B. Hoek, J. Peterson, and A. Cahill (2003)
Nucleic Acids Res. 31, 1364-1373
   Abstract »    Full Text »    PDF »
Endonuclease G, a Candidate Human Enzyme for the Initiation of Genomic Inversion in Herpes Simplex Type 1 Virus.
K.-J. Huang, B. V. Zemelman, and I. R. Lehman (2002)
J. Biol. Chem. 277, 21071-21079
   Abstract »    Full Text »    PDF »
Action of Recombinant Human Apoptotic Endonuclease G on Naked DNA and Chromatin Substrates. COOPERATION WITH EXONUCLEASE AND DNase I.
P. Widlak, L. Y. Li, X. Wang, and W. T. Garrard (2001)
J. Biol. Chem. 276, 48404-48409
   Abstract »    Full Text »    PDF »
The expanding role of mitochondria in apoptosis.
X. Wang (2001)
Genes & Dev. 15, 2922-2933
   Full Text »    PDF »
Mitochondrial Release of Caspase-2 and -9 during the Apoptotic Process.
S. A. Susin, H. K. Lorenzo, N. Zamzami, I. Marzo, C. Brenner, N. Larochette, M.-C. Prevost, P. M. Alzari, and G. Kroemer (1999)
J. Exp. Med. 189, 381-394
   Abstract »    Full Text »    PDF »
On the Advantage of Being a Dimer, a Case Study Using the Dimeric Serratia Nuclease and the Monomeric Nuclease from Anabaena sp. Strain PCC 7120.
I. Franke, G. Meiss, and A. Pingoud (1999)
J. Biol. Chem. 274, 825-832
   Abstract »    Full Text »    PDF »
Initiation of Mitochondrial DNA Replication by Transcription and R-loop Processing.
D. Y. Lee and D. A. Clayton (1998)
J. Biol. Chem. 273, 30614-30621
   Abstract »    Full Text »    PDF »
Transcription-Dependent DNA Transactions in the Mitochondrial Genome of a Yeast Hypersuppressive Petite Mutant.
E. Van Dyck and D. A. Clayton (1998)
Mol. Cell. Biol. 18, 2976-2985
   Abstract »    Full Text »
RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication..
D Y Lee and D A Clayton (1997)
Genes & Dev. 11, 582-592
   Abstract »    PDF »
The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins..
Z Lygerou, P Mitchell, E Petfalski, B Seraphin, and D Tollervey (1994)
Genes & Dev. 8, 1423-1433
   Abstract »    PDF »



ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)