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J Biol Chem, Vol. 274, Issue 34, 23687-23690, August 20, 1999

COMMUNICATION
A Novel BH3-like Domain in BID Is Required for Intramolecular Interaction and Autoinhibition of Pro-apoptotic Activity

Kuan Onn Tan, Karen Mei Ling Tan, and Victor C. Yu

From the Institute of Molecular and Cell Biology, National University of Singapore, 30 Medical Drive, Singapore 117609, Republic of Singapore

Upon activation of the Fas apoptotic signaling pathway, Bid, a "BH3 domain-only" pro-apoptotic molecule, is cleaved by caspase-8 into a 6.5-kDa N-terminal and a 15-kDa BH3 domain-containing C-terminal fragment, referred to as tn-Bid and tc-Bid, respectively. tc-Bid is a more potent inducer of apoptosis than full-length Bid, suggesting that the N-terminal region of Bid has an inhibitory effect on its pro-apoptotic activity. Here, we report the identification of a novel BH3-like motif (amino acid residues 35-43) in tn-Bid. Although Bid does not homodimerize, tn-Bid is able to associate avidly with tc-Bid. Site-directed mutagenesis revealed that both the novel BH3-like and BH3 domains are necessary for direct binding between tn-Bid and tc-Bid. While full-length Bid does not associate with tn-Bid, substitution of Leu35, a critical residue in mediating tn-Bid/tc-Bid interaction, with Ala in full-length Bid is sufficient to establish Bid/tn-Bid interaction. Interestingly, the L35A Bid mutant is as effective as tc-Bid in inducing apoptosis and binding Bcl-XL. We propose that the intramolecular interaction involving the BH3-like and BH3 domains serves to regulate the pro-apoptotic potential of Bid.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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