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Microbiology and Molecular Biology Reviews, March 2000, p. 13-33, Vol. 64, No. 1
1092-2172/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Membrane Topology and Insertion of Membrane Proteins: Search for Topogenic Signals

Marleen van Geest and Juke S. Lolkema*

Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands

Integral membrane proteins are found in all cellular membranes and carry out many of the functions that are essential to life. The membrane-embedded domains of integral membrane proteins are structurally quite simple, allowing the use of various prediction methods and biochemical methods to obtain structural information about membrane proteins. A critical step in the biosynthetic pathway leading to the folded protein in the membrane is its insertion into the lipid bilayer. Understanding of the fundamentals of the insertion and folding processes will significantly improve the methods used to predict the three-dimensional membrane protein structure from the amino acid sequence. In the first part of this review, biochemical approaches to elucidate membrane protein topology are reviewed and evaluated, and in the second part, the use of similar techniques to study membrane protein insertion is discussed. The latter studies search for signals in the polypeptide chain that direct the insertion process. Knowledge of the topogenic signals in the nascent chain of a membrane protein is essential for the evaluation of membrane topology studies.

* Corresponding author. Mailing address: Department of Microbiology, University of Groningen Biological Center, Kerklaan 30, 9751 NN Haren, The Netherlands. Phone: 3150-3532155. Fax: 3150-3632154. E-mail: j.s.lolkema{at}biol.rug.nl.

Microbiology and Molecular Biology Reviews, March 2000, p. 13-33, Vol. 64, No. 1
1092-2172/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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