characterization of the proteasome from the extremely halophilic archaeon haloarcula marismortui描述的蛋白酶体极端嗜盐的archaeon haloarcula marismortui.pdfVIP

Archaea 1, 53–61 © 2002 Heron Publishing—Victoria, Canada Characterization of the proteasome from the extremely halophilic archaeon Haloarcula marismortui 1,2 3 1 3 1 B. FRANZETTI, G. SCHOEHN, D. GARCIA, R. W. H. RUIGROK and G. ZACCAI 1 Institut de Biologie Structurale, CNRS-CEA, 41 rue J. Horowitz, 38027 Grenoble cedex 1, France 2 Author to whom correspondence should be addressed (franzetti@ibs.fr) 3 EMBL Grenoble Outstation, EMBL, PB156, 38042 Grenoble cedex 9, France Received August 22, 2001; accepted October 22, 2001; published online November 15, 2001 Summary A 20S proteasome, comprising two subunits α al. 1998). An extensive study of malate dehydrogenase from and β, was purified from the extreme halophilic archaeon Haloarcula marismortui has led to the conclusion that hy- Haloarcula marismortui, which grows only in saturated salt drated salt ions are associated with acidic residues situated on conditions. The three-dimensional reconstruction of the the protein surface in such a way that the salt concentration of H. marismortui proteasome (Hm proteasome), obtained from the solvation layer is higher than that of the bulk solvent (Bon- negatively stained electron micrographs, is virtually identical nete et al. 1994, Madern et al. 1995, Ebel et al. 1999). It was to the structure of a thermophilic proteasome filtered to the suggested that this characteristic allows halophilic proteins to same resolution. The stability of the Hm proteasome was found remain stable and soluble in high salt concentrations (Zaccai et to be less salt-dependent than that of other halophilic enzymes