Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1784, Issue 5, Pages 727-735Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2008.02.010
Keywords
oligomeric ATP-dependent proteases; protein; peptide; mechanism
Categories
Funding
- NIGMS NIH HHS [R01 GM067172, R01 GM067172-05, GM067172, GM61095, R01 GM061095] Funding Source: Medline
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Lon, also known as the protease La, is a homo-oligomericATP-dependent protease,which is highly conserved in archaea, eubacteria and eukaryotic mitochondria and peroxisomes. Since its discovery, studies have shown that Lon activity is essential for cellular homeostasis, mediating protein quality control and metabolic regulation. This article highlights the discoveries made over the past decade demonstrating that Lon selectively degrades abnormal as well as certain regulatory proteins and thus plays significant roles in maintaining bacterial and mitochondrial function and integrity. in addition, Lon is required in certain pathogenic bacteria, for rendering pathogenicity and host infectivity. Recent research endeavors have been directed toward elucidating the reaction mechanism of the Lon protease by different biochemical and structural biological techniques. In this mini-review, the authors survey the diverse biological roles of Lon, and also place special emphasis on recent findings that clarify the mechanistic aspects of the Lon reaction cycle. (c) 2008 Elsevier B.V. All rights reserved.
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