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Science 26 September 1986: Vol. 233. no. 4771, pp. 1403 - 1408 DOI: 10.1126/science.3529391
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Articles
Science, Vol 233, Issue 4771, 1403-1408
Copyright © 1986 by American Association for the Advancement of Science
A genetic approach to analyzing membrane protein topology
C Manoil
and
J Beckwith
Fusions of the secreted protein alkaline phosphatase to an integral cytoplasmic membrane protein of Escherichia coli showed different activities depending on where in the membrane protein the alkaline phosphatase was fused. Fusions to positions in or near the periplasmic domain led to high alkaline phosphatase activity, whereas those to positions in the cytoplasmic domain gave low activity. Analysis of alkaline phosphatase fusions to membrane proteins of unknown structure may thus be generally useful in determining their membrane topologies.
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