Oligomeric structure of the ATP-dependent protease La(Lon) of Escherichia coli

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Lon, also known as protease La, belongs to a class of ATP-dependent serine protease. It plays an essential role in degradation of abnormal proteins and of certain short-lived regulatory proteins, and is thought to possess a Ser-Lys catalytic dyad. To examine the structural organization of Lon, we performed an electron microscope analysis. The averaged images of Lon with end-on orientation revealed a six-membered, ring-shaped structure with a central cavity. The side-on view showed a two-layered structure with an equal distribution of mass across the equatorial plane of the complex. Since a Lon subunit possesses two large regions containing nucleotide binding and proteolytic domains, each layer of the Lon hexamer appears to consist of the side projections of one of the major domains arranged in a ring. Lon showed a strong tendency to form hexamers in the presence of Mg2+, but dissociated into monomers and/or dimers in its absence. Moreover, Mg2+-dependent hexamer formation was independent of ATP. These results indicate that Lon has a hexameric ring-shaped structure with a central cavity, and that the establishment of this configuration requires Mg2+, but not ATP.
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Issue Date
2006-02
Language
English
Article Type
Article
Citation

MOLECULES AND CELLS, v.21, no.1, pp.129 - 134

ISSN
1016-8478
URI
http://hdl.handle.net/10203/89292
Appears in Collection
CH-Journal Papers(저널논문)
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