Mitochondrial Lon of Saccharomyces Cerevisiae Is a Ring-Shaped Protease with Seven Flexible Subunits

Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible ring-shaped heptamer. In the presence of ATP or 5′-adenylylimidodiphosphate, most of the rings are symmet...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1999-06, Vol.96 (12), p.6787-6790
Main Authors: Stahlberg, Henning, Kutejova, Eva, Suda, Kitaru, Wolpensinger, Bettina, Lustig, Ariel, Schatz, Gottfried, Engel, Andreas, Suzuki, Carolyn K.
Format: Article
Language:English
Subjects:
Adenosine triphosphatases
ATP-Dependent Proteases
Average linear density
Biological Sciences
Cell biology
Cellular biology
Crosslinking
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Fungal Proteins - ultrastructure
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Heat-Shock Proteins - ultrastructure
Microscopy, Electron
Mitochondria - enzymology
Nucleotides
Optics
Protein Folding
Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - ultrastructure
Serine Endopeptidases - chemistry
Serine Endopeptidases - metabolism
Serine Endopeptidases - ultrastructure
Transmission electron microscopy
Ultracentrifugation
Yeast
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Summary:Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible ring-shaped heptamer. In the presence of ATP or 5′-adenylylimidodiphosphate, most of the rings are symmetric and resemble other ATP-driven machines that mediate folding and degradation of proteins. In the absence of nucleotides, most of the rings are distorted, with two adjacent subunits forming leg-like protrusions. These results suggest that asymmetric conformational changes serve to power processive unfolding and translocation of substrates to the active site of the Lon protease.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.12.6787