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Biochemistry. 1991 Mar 26;30(12):3082-8.

Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: high-level expression in Escherichia coli.

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Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.


The integral membrane protein bacterioopsin, found in the extremely halophilic archaebacterium Halobacterium halobium, was expressed in Escherichia coli as a fusion protein containing 13 heterologous amino acids at the amino terminus. The expressed protein was localized primarily to the E. coli cytoplasmic membrane (greater than 80%) and had an in vivo half-life of 26 min. The amount of bacterioopsin in E. coli crude lysates was quantitated immunologically from Western blots and was expressed at 10-20-fold higher levels than seen previously (i.e., 17 mg/L; 5.6% of the total protein). Three distinct forms of the protein were detected immunologically: two of the forms were generated by the removal of either one or four amino acid residues at the amino terminus; the third form remained unaltered.

[Indexed for MEDLINE]

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