Abstract
Voltage-gated potassium channel modulatory membrane proteinKCNE3 was overexpressed and purified into both micelles and bicelles. Remarkably, microinjection of KCNE3 in bicelles into Xenopus oocytes resulted in functional co-assembly with the human KCNQ1 channel expressed therein. Microinjection of LMPC micelles containing KCNE3 did not result in channel modulation, indicating that bicelles sometimes succeed at delivering a membrane protein into a cellular membrane when classical micelles fail. Backbone NMR resonance assignments were completed for KCNE3 in both bicelles and LMPC, indicating that the secondary structure distribution in KCNE3's N-terminus and transmembrane domains exhibits only modest differences from that of KCNE1, even though these KCNE family members have very different effects on KCNQ1 channel function.
Original language | English (US) |
---|---|
Pages (from-to) | 653-655 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 49 |
Issue number | 4 |
DOIs | |
State | Published - Feb 2 2010 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry