Structural requirements for membrane assembly of proteins spanning the membrane several times.
Open Access
- 1 November 1989
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 109 (5) , 2013-2022
- https://doi.org/10.1083/jcb.109.5.2013
Abstract
We have investigated the structural requirements for the biogenesis of proteins spanning the membrane several times. Proteins containing various combinations of topological signals (signal anchor and stop transfer sequences) were synthesized in a cell-free translation system and their membrane topology was determined. Proteins spanning the membrane twice were obtained when a signal anchor sequence was followed by either a stop transfer sequence or a second signal anchor sequence. Thus, a signal anchor sequence in the second position can function as a stop transfer sequence, spanning the membrane in the opposite orientation to that of the first signal anchor sequence. A signal anchor sequence in the third position was able to insert amino acid sequences located COOH terminal to it. We conclude that proteins spanning the membrane several times can be generated by stringing together signal anchor and stop transfer sequences. However, not all proteins with three topological signals were found to span the membrane three times. A certain segment located between the first and second topological signal could prevent stable membrane integration of a third signal anchor segment.This publication has 39 references indexed in Scilit:
- PrlC, a suppressor of signal sequence mutations in Escherichia coli, can direct the insertion of the signal sequence into the membraneJournal of Molecular Biology, 1989
- Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequenceCell, 1988
- A signal sequence receptor in the endoplasmic reticulum membraneNature, 1987
- Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane bindingCell, 1987
- A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membraneCell, 1986
- The membrane-spanning segment of invariant chain (Iγ) contains a potentially cleavable signal sequenceCell, 1986
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Dual functions of the signal peptide in protein transfer across the membraneCell, 1985
- Structure and biosynthesis of histocompatibility antigens (H-2, HLA)Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970