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== Function ==
== Function ==
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The mitochondrial Lon protease is an important regulator of mitochondrial [https://en.wikipedia.org/wiki/Metabolism metabolism] including the maintenance and repair of mitochondrial [https://en.wikipedia.org/wiki/DNA DNA], the homeostasis of mitochondria, and by regulating some regulatory proteins which have a short life or damaged proteins.
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The mitochondrial Lon protease is an important regulator of mitochondrial [https://en.wikipedia.org/wiki/Metabolism metabolism] including the maintenance and repair of mitochondrial [https://en.wikipedia.org/wiki/DNA DNA]. This protein is also essential for homeostasis of mitochondria, and by regulating some regulatory proteins which have a short life or damaged proteins.
Lon protease has three main roles.
Lon protease has three main roles.
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Lon protease is involved in [https://en.wikipedia.org/wiki/Mitochondrial_DNA mtDNA] [https://en.wikipedia.org/wiki/DNA_replication replication] and [https://en.wikipedia.org/w/index.php?title=Mitogenesis&redirect=no mitogenesis] by being a '''mitochondrial [https://en.wikipedia.org/wiki/DNA-binding_protein DNA-bing protein]'''.
Lon protease is involved in [https://en.wikipedia.org/wiki/Mitochondrial_DNA mtDNA] [https://en.wikipedia.org/wiki/DNA_replication replication] and [https://en.wikipedia.org/w/index.php?title=Mitogenesis&redirect=no mitogenesis] by being a '''mitochondrial [https://en.wikipedia.org/wiki/DNA-binding_protein DNA-bing protein]'''.
Mitochondrial Lon protease interacts with [https://en.wikipedia.org/wiki/Chaperone_(protein) protein chaperone], notably [https://en.wikipedia.org/wiki/Chaperonin HSP60]-[https://en.wikipedia.org/wiki/Hsp70 Hsp70] complex to protect cell from apoptosis under environmental stress<ref>Bota, Daniela A., and Kelvin J. A. Davies. “Mitochondrial Lon Protease in Human Disease and Aging: Including an Etiologic Classification of Lon-Related Diseases and Disorders.” Free Radical Biology & Medicine 100 (November 2016): 188–98. https://doi.org/10.1016/j.freeradbiomed.2016.06.031.</ref>.
Mitochondrial Lon protease interacts with [https://en.wikipedia.org/wiki/Chaperone_(protein) protein chaperone], notably [https://en.wikipedia.org/wiki/Chaperonin HSP60]-[https://en.wikipedia.org/wiki/Hsp70 Hsp70] complex to protect cell from apoptosis under environmental stress<ref>Bota, Daniela A., and Kelvin J. A. Davies. “Mitochondrial Lon Protease in Human Disease and Aging: Including an Etiologic Classification of Lon-Related Diseases and Disorders.” Free Radical Biology & Medicine 100 (November 2016): 188–98. https://doi.org/10.1016/j.freeradbiomed.2016.06.031.</ref>.
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The mitochondrial Lon protease is essentially found in the cytoplasmic of mitochondria because [https://en.wikipedia.org/wiki/Amino_acid amino-acid] has a potential mitochondrial targetting presequences.

Revision as of 16:49, 12 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
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2x36 - Structure of the proteolytic domain of the Human Mitochondrial Lon protease

Caption for this structure

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ Bota, Daniela A., and Kelvin J. A. Davies. “Mitochondrial Lon Protease in Human Disease and Aging: Including an Etiologic Classification of Lon-Related Diseases and Disorders.” Free Radical Biology & Medicine 100 (November 2016): 188–98. https://doi.org/10.1016/j.freeradbiomed.2016.06.031.
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