Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli.
The two genes encoding the constituent subunits of the Thermoplasma acidophilum proteasome were expressed in Escherichia coli yielding fully assembled molecules as shown by electron microscopy. The recombinant proteasomes were purified to homogeneity and were shown to have proteolytic activity indistinguishable from proteasomes isolated from T. acidophilum.
Zwickl
P
P
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Lottspeich
F
F
Baumeister
W
W
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D004269:DNA, Bacterial; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013822:Thermoplasma / Q000201:enzymology / Q000235:genetics*
D004269:DNA, Bacterial; D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex