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The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans‐membrane topology
Author(s) -
Heijne Gunnar
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04601.x
Subject(s) - periplasmic space , biology , inner membrane , cytosol , biogenesis , membrane protein , membrane topology , membrane , biochemistry , biophysics , amino acid , bacterial outer membrane , microbiology and biotechnology , topology (electrical circuits) , escherichia coli , enzyme , mathematics , combinatorics , gene
The amino acid distribution in membrane spanning segments and connecting loops in bacterial inner membrane proteins was analysed. The basic residues Arg and Lys are four times less prevalent in periplasmic as compared to cytosolic connecting loops, whereas no comparable effect is observed for the acidic residues Asp and Glu. Also, Pro is shown to be tolerated to a much larger extent in membrane spanning segments with their N‐terminus pointing towards the cytosol than in those with the opposite orientation. The significance of these findings with regard to the mechanism of biogenesis of bacterial inner membrane proteins is discussed.