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Protein Engineering, Vol. 13, No. 12, 887-892, December 2000
© 2000 Oxford University Press

Non-ionic detergent affects the conformation of a functionally active mutant of Bcl-XL

Yee-Joo Tan,1 and Anthony E. Ting

Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Republic of Singapore

We found that a mutant, Bcl-XL(F131V), which was previously reported to have impaired binding capacity, can bind to Bax almost as strongly as wild-type Bcl-XL. In the absence of detergent, the Bcl-XL(F131V) mutant adopts the same conformation as wild-type Bcl-XL, as determined by circular dichroism spectroscopy and size-exclusion chromatography. However, non-ionic detergent induces a conformational change in the Bcl-XL(F131V) mutant and causes it to lose Bax-binding capacity. Wild-type Bcl-XL, on the other hand, is more resistant to detergent-induced effects and retains its ability to bind Bax in the presence of detergent. Since it has been shown that the Bcl-XL(F131V) mutant has nearly the same anti-apoptotic activity as wild-type Bcl-XL, it would be likely that the Bcl-XL(F131V) mutant can adopt the wild-type conformation, rather than the detergent-induced conformational state and can bind to Bax in vivo. Therefore, our data demonstrated that non-ionic detergent can have unpredicted effects on protein conformation, differential effects on wild-type and mutant Bcl-XL proteins in this case and may cause complications in the interpretation of in vitro binding studies.


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