Multitasking in the mitochondrion by the ATP-dependent Lon protease

Sundararajan Venkatesh, Jae Lee, Kamalendra Singh, Irene Lee, Carolyn K. Suzuki

Research output: Contribution to journalReview articlepeer-review

114 Scopus citations

Abstract

The AAA + Lon protease is a soluble single-ringed homo-oligomer, which represents the most streamlined operational unit mediating ATP-dependent proteolysis. Despite its simplicity, the architecture of Lon proteases exhibits a species-specific diversity. Homology modeling provides insights into the structural features that distinguish bacterial and human Lon proteases as hexameric complexes from yeast Lon, which is uniquely heptameric. The best-understood functions of mitochondrial Lon are linked to maintaining proteostasis under normal metabolic conditions, and preventing proteotoxicity during environmental and cellular stress. An intriguing property of human Lon is its specific binding to G-quadruplex DNA, and its association with the mitochondrial genome in cultured cells. A fraction of Lon preferentially binds to the control region of mitochondrial DNA where transcription and replication are initiated. Here, we present an overview of the diverse functions of mitochondrial Lon, as well as speculative perspectives on its role in protein and mtDNA quality control. This article is part of a Special Issue entitled: AAA ATPases: structure and function.

Original languageEnglish (US)
Pages (from-to)56-66
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1823
Issue number1
DOIs
StatePublished - Jan 2012

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Keywords

  • AAA
  • ATP-dependent protease
  • Lon
  • Mitochondria
  • MtDNA
  • Unfolded protein response (UPR)

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