MMBR Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by van Geest, M.
Right arrow Articles by Lolkema, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by van Geest, M.
Right arrow Articles by Lolkema, J. S.

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.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. J. Bacteriol.
ALL ASM JOURNALS

Copyright © 2000 by the American Society for Microbiology. All rights reserved.