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Volume 271, Number 44, Issue of November 1, 1996 pp. 27245-27248
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Functional Characterization of the Prodomain of Interleukin1beta -converting Enzyme

(Received for publication, July 25, 1996, and in revised form, September 11, 1996)

Wim Van Criekinge , Rudi Beyaert , Marc Van de Craen , Peter Vandenabeele , Peter Schotte , Dirk De Valck and Walter Fiers

From the Laboratory of Molecular Biology, Flanders Interuniversity Institute for Biotechnology and University of Ghent, B-9000 Ghent, Belgium

Interleukin-1beta -converting enzyme (ICE) has been identified as the main protease responsible for maturation of the prodomain of interleukin-1beta . Recently, it was shown to belong to a larger gene family, members of which play an important role in programmed cell death. A common feature of the ICE family proteases is the presence of a prodomain that has been hypothesized to keep the enzyme in an inactive form. Expression analysis in yeast revealed autocatalytic degradation of p45ICE, but not of p30ICE lacking a prodomain. We further demonstrate that p45ICE, in which the critical cysteine has been mutated, is still able to dimerize in vivo. Dimerization requires the prodomain and occurs prior to autoprocessing. These results provide evidence for a regulatory role of the prodomain of ICE.


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