TY - JOUR
T1 - Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
AU - Lee, Irene
AU - Suzuki, Carolyn K.
N1 - Funding Information:
The work described in the authors' lab was supported by the National Institutes of Health (GM61095), the Basil O'Connor Scholars Award - March of Dimes and the American Heart Association to C. K. Suzuki; the National Institutes of Health (GM067172) to I. Lee.
PY - 2008/5
Y1 - 2008/5
N2 - Lon, also known as the protease La, is a homo-oligomeric ATP-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.
AB - Lon, also known as the protease La, is a homo-oligomeric ATP-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.
KW - Mechanism
KW - Oligomeric ATP-dependent proteases
KW - Peptide
KW - Protein
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U2 - 10.1016/j.bbapap.2008.02.010
DO - 10.1016/j.bbapap.2008.02.010
M3 - Review article
C2 - 18359303
AN - SCOPUS:41949134709
SN - 1570-9639
VL - 1784
SP - 727
EP - 735
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 5
ER -