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J. Biol. Chem., Vol. 268, Issue 20, 14682-14686, Jul, 1993

The N-terminal hydrophobic domain of P450c21 is required for membrane insertion and enzyme stability

LC Hsu, MC Hu, HC Cheng, JC Lu and BC Chung
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China.

Microsomal cytochromes P-450 are known to be integrated into smooth endoplasmic reticulum through their hydrophobic sequences located at the N termini. The length requirement of the membrane insertion signal was determined by the generation of six plasmids encoding mutant P450c21 that lacked various portions of the N-terminal hydrophobic domains. When they were transcribed and translated in vitro in the presence of endoplasmic reticulum membranes, mutant protein lacking more than a third of the first hydrophobic domain gradually lost the ability to insert into the membrane and stayed mostly in the soluble fraction when the first N-terminal hydrophobic domain was removed. The steady-state amount of the truncated proteins was progressively reduced in parallel to the extent of their N-terminal deletions, due to their fast degradation. This process was accompanied by a decrease in the enzymatic activity. Therefore, the first hydrophobic domain of P450c21 not only serves as a membrane targeting and anchoring domain, but it is also important for the in vivo protein stability.
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