Abstract

Interleukin-1 beta converting enzyme (ICE) is composed of 10' (p10) and 20 kDa (p20) subunits, which are derived from a common 45 kDa precursor. Recent crystallographic studies have shown that ICE exists as a tetramer (p20/p10)2 in the crystal lattice. We provide evidence that the p10 and p20 subunits of ICE associate as oligomers in transfected COS cells. Using intragenic complementation, we show that the activity of a p10/p10 interface mutant defective in autoprocessing can be restored by co-expression with active site ICE mutants. Different active site mutants can also complement each other by oligomerization to form active ICE. These studies indicate that ICE precursor polypeptides may associate in different quaternary structures and that oligomerization is required for autoprocessing. Furthermore, integenic complementation of active site mutants of ICE and an ICE homolog restores autoprocessing activity, suggesting that hetero-oligomerization occurs between ICE homologs.

Keywords

BiologyIn vivoEnzymeBiochemistryBETA (programming language)Enzyme assayMolecular biologyGenetics

MeSH Terms

Amino Acid SequenceAnimalsBase SequenceBinding SitesCaspase 1Cell LineCysteine EndopeptidasesDNAComplementaryGenetic Complementation TestHumansModelsMolecularMolecular Sequence DataMutationProtein ConformationProtein ProcessingPost-TranslationalTransfection

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Publication Info

Year
1995
Type
article
Volume
14
Issue
9
Pages
1923-1931
Citations
133
Access
Closed

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Cite This

Yun Gu, Wu Junwei, Chi Faucheu et al. (1995). Interleukin-1 beta converting enzyme requires oligomerization for activity of processed forms in vivo.. The EMBO Journal , 14 (9) , 1923-1931. https://doi.org/10.1002/j.1460-2075.1995.tb07184.x

Identifiers

DOI
10.1002/j.1460-2075.1995.tb07184.x
PMID
7743999
PMCID
PMC398291

Data Quality

Data completeness: 86%