Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Oligomeric Structure of the ATP-dependent Protease La (Lon) of Escherichia coli

  • Park, Seong-Cheol (Division of Applied Life Science, Gyeongsang National University) ;
  • Jia, Baolei (Division of Applied Life Science, Gyeongsang National University) ;
  • Yang, Jae-Kyung (Faculty of Forest Science, Gyeongsang National University) ;
  • Le Van, Duyet (Division of Applied Life Science, Gyeongsang National University) ;
  • Shao, Yong Gi (Division of Applied Life Science, Gyeongsang National University) ;
  • Han, Sang Woo (Department of Chemistry, Gyeongsang National University) ;
  • Jeon, Young-Joo (NRL of Protein Biochemistry, School of Biological Science, Seoul National University) ;
  • Chung, Chin Ha (NRL of Protein Biochemistry, School of Biological Science, Seoul National University) ;
  • Cheong, Gang-Won (Division of Applied Life Science, Gyeongsang National University)
  • Received : 2005.09.21
  • Accepted : 2005.10.27
  • Published : 2006.02.28
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Abstract

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 $Mg^{2+}$, but dissociated into monomers and/or dimers in its absence. Moreover, $Mg^{2+}$-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 $Mg^{2+}$, but not ATP.

Keywords

Acknowledgement

Supported by : Korea Science and Engineering Foundation

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