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Science 13 February 1987:
Vol. 235. no. 4790, pp. 783 - 787
DOI: 10.1126/science.3544218
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Articles

Science, Vol 235, Issue 4790, 783-787
Copyright © 1987 by American Association for the Advancement of Science

articles

Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly

RE Dalbey and W Wickner

Leader peptidase spans the Escherichia coli plasma membrane with its amino-terminal domain facing the cytoplasm and its carboxyl terminus facing the periplasm. It is made without a cleavable leader sequence. The three apolar domains near the amino terminus of the peptidase are candidates for internal "signal sequences" and they anchor the protein to the lipid bilayer. Oligonucleotide-directed deletion was used to show that only the second domain has an essential function in membrane assembly. While this second apolar domain is crucial for membrane assembly, its continued function when disrupted by arginine suggests that its apolar character per se is not its only important feature.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Insertion of Leader Peptidase into the Thylakoid Membrane during Synthesis in a Chloroplast Translation System.
E. Houben, J.-W. de Gier, and K. J. van Wijk (1999)
PLANT CELL 11, 1553-1564
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The SecA Subunit of Escherichia coli Preprotein Translocase Is Exposed to the Periplasm.
J. Eichler and W. Wickner (1998)
J. Bacteriol. 180, 5776-5779
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Multidrug Resistance Protein. IDENTIFICATION OF REGIONS REQUIRED FOR ACTIVE TRANSPORT OF LEUKOTRIENE C4.
M. Gao, M. Yamazaki, D. W. Loe, C. J. Westlake, C. E. Grant, S. P. C. Cole, and R. G. Deeley (1998)
J. Biol. Chem. 273, 10733-10740
   Abstract »    Full Text »    PDF »
SecA-independent Translocation of the Periplasmic N-terminal Tail of an Escherichia coli Inner Membrane Protein.
P. Whitley, G. Gafvelin, and G. von Heijne (1995)
J. Biol. Chem. 270, 29831-29835
   Abstract »    Full Text »    PDF »


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