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Science 12 February 1999:
Vol. 283. no. 5404, pp. 978 - 981
DOI: 10.1126/science.283.5404.978
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Reports

A Giant Protease with Potential to Substitute for Some Functions of the Proteasome

Elke Geier, 1 Günter Pfeifer, 2 Matthias Wilm, 3 Maria Lucchiari-Hartz, 1 Wolfgang Baumeister, 2 Klaus Eichmann, 1 Gabriele Niedermann 1*

An alanyl-alanyl-phenylalanyl-7-amino-4-methylcoumarin-hydrolyzing protease particle copurifying with 26S proteasomes was isolated and identified as tripeptidyl peptidase II (TPPII), a cytosolic subtilisin-like peptidase of unknown function. The particle is larger than the 26S proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage. TPPII may thus participate in extralysosomal polypeptide degradation and may in part account for nonproteasomal epitope generation as postulated for certain major histocompatibility complex class I alleles. In addition, TPPII may be able to substitute for some metabolic functions of the proteasome.

1 Max-Planck Institute of Immunobiology, Stübeweg 51, D-79108 Freiburg, Germany.
2 Max-Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
3 European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
*   To whom correspondence should be addressed. E-mail: niedermann{at}immunbio.mpg.de

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